HEADER HYDROLASE 30-JUL-19 6KLK
TITLE CRYSTAL STRUCTURE OF THE PSEUDOMONAS AERUGINOSA DIHYDROPYRIMIDINASE
TITLE 2 COMPLEXED WITH 5-FU
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-HYDANTOINASE/DIHYDROPYRIMIDINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DHPASE;
COMPND 5 EC: 3.5.2.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 / DSM
SOURCE 3 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 6 / 1C / PRS 101 / PAO1;
SOURCE 7 GENE: DHT, PA0441;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, DIHYDROPYRIMIDINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.H.HUANG,I.C.CHEN,C.Y.HUANG
REVDAT 2 22-NOV-23 6KLK 1 LINK
REVDAT 1 06-NOV-19 6KLK 0
JRNL AUTH Y.H.HUANG,Z.J.NING,C.Y.HUANG
JRNL TITL CRYSTAL STRUCTURE OF DIHYDROPYRIMIDINASE IN COMPLEX WITH
JRNL TITL 2 ANTICANCER DRUG 5-FLUOROURACIL.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 519 160 2019
JRNL REFN ESSN 1090-2104
JRNL PMID 31481233
JRNL DOI 10.1016/J.BBRC.2019.08.153
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 113950
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 5674
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 5.4518 - 4.3325 0.99 3665 222 0.1439 0.1478
REMARK 3 2 4.3325 - 3.7864 1.00 3649 214 0.0000 0.1756
REMARK 3 3 3.7864 - 3.4409 1.00 3669 188 0.0000 0.1741
REMARK 3 4 3.4409 - 3.1946 1.00 3618 174 0.0000 0.1921
REMARK 3 5 3.1946 - 3.0065 1.00 3627 204 0.0000 0.2169
REMARK 3 6 3.0065 - 2.8561 1.00 3591 207 0.0000 0.2394
REMARK 3 7 2.8561 - 2.7319 1.00 3638 204 0.0000 0.2198
REMARK 3 8 2.7319 - 2.6268 1.00 3607 203 0.0000 0.2345
REMARK 3 9 2.6268 - 2.5362 1.00 3543 221 0.0000 0.2137
REMARK 3 10 2.5362 - 2.4570 1.00 3622 186 0.0000 0.2347
REMARK 3 11 2.4570 - 2.3868 1.00 3619 163 0.0000 0.2201
REMARK 3 12 2.3868 - 2.3240 1.00 3621 153 0.0000 0.2184
REMARK 3 13 2.3240 - 2.2673 1.00 3604 191 0.0000 0.2434
REMARK 3 14 2.2673 - 2.2158 1.00 3597 172 0.0000 0.2208
REMARK 3 15 2.2158 - 2.1687 1.00 3622 206 0.0000 0.2251
REMARK 3 16 2.1687 - 2.1253 1.00 3608 164 0.0000 0.2236
REMARK 3 17 2.1253 - 2.0852 1.00 3582 188 0.0000 0.2685
REMARK 3 18 2.0852 - 2.0480 1.00 3575 178 0.0000 0.2287
REMARK 3 19 2.0480 - 2.0133 1.00 3580 202 0.0000 0.2714
REMARK 3 20 2.0133 - 1.9808 1.00 3570 195 0.0000 0.2287
REMARK 3 21 1.9808 - 1.9503 1.00 3555 177 0.0000 0.2728
REMARK 3 22 1.9503 - 1.9217 1.00 3604 198 0.0000 0.2605
REMARK 3 23 1.9217 - 1.8946 1.00 3581 162 0.0000 0.2878
REMARK 3 24 1.8946 - 1.8690 1.00 3611 185 0.0000 0.2594
REMARK 3 25 1.8690 - 1.8447 1.00 3599 158 0.0000 0.2789
REMARK 3 26 1.8447 - 1.8217 1.00 3539 184 0.0000 0.2698
REMARK 3 27 1.8217 - 1.7997 1.00 3596 176 0.0000 0.2979
REMARK 3 28 1.7997 - 1.7788 1.00 3588 178 0.0000 0.2532
REMARK 3 29 1.7788 - 1.7590 1.00 3546 213 0.0000 0.3244
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.19
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 6KLK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1300013218.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 298
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 : BL13C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.975
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114045
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.759
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.47100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: 5E5C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18%PEG8000, 100MM HEPES PH7.5, 200MM
REMARK 280 CALCIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.32567
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 106.65133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 106.65133
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 53.32567
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 757 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 816 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 863 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 900 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 710 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 792 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 1
REMARK 465 MET B 1
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 OE2 GLU B 132 NH2 ARG B 135 2.19
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 12 -169.16 -109.56
REMARK 500 HIS A 59 83.37 -150.54
REMARK 500 GLN A 63 41.82 36.80
REMARK 500 ALA A 154 -161.81 -109.89
REMARK 500 ASN A 157 4.01 57.70
REMARK 500 ALA A 158 -110.78 -114.91
REMARK 500 ARG A 212 65.70 -150.37
REMARK 500 HIS A 239 70.18 21.33
REMARK 500 ASP A 331 102.05 -163.37
REMARK 500 SER A 369 -53.08 -145.12
REMARK 500 GLN B 63 44.14 38.99
REMARK 500 ASP B 92 -169.35 -103.32
REMARK 500 ALA B 154 -162.36 -109.28
REMARK 500 ALA B 158 -98.71 -131.32
REMARK 500 ARG B 212 67.08 -157.78
REMARK 500 HIS B 239 69.27 24.92
REMARK 500 HIS B 317 104.31 -58.30
REMARK 500 ASP B 331 97.96 -169.38
REMARK 500 SER B 369 -53.20 -147.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 122 HIS A 123 147.14
REMARK 500 PHE B 122 HIS B 123 146.32
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 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 59 NE2
REMARK 620 2 HIS A 61 NE2 102.9
REMARK 620 3 KCX A 150 OQ2 92.1 89.6
REMARK 620 4 ASP A 316 OD1 87.6 90.6 179.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 150 OQ1
REMARK 620 2 HIS A 183 ND1 103.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 59 NE2
REMARK 620 2 HIS B 61 NE2 104.6
REMARK 620 3 KCX B 150 OQ2 87.7 83.4
REMARK 620 4 ASP B 316 OD1 85.6 93.6 171.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 150 OQ1
REMARK 620 2 HIS B 183 ND1 99.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue URF A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 502
DBREF 6KLK A 1 479 UNP Q9I676 HYDA_PSEAE 1 479
DBREF 6KLK B 1 479 UNP Q9I676 HYDA_PSEAE 1 479
SEQRES 1 A 479 MET SER LEU LEU ILE ARG GLY ALA THR VAL VAL THR HIS
SEQRES 2 A 479 GLU GLU SER TYR ARG ALA ASP VAL LEU CYS ALA ASN GLY
SEQRES 3 A 479 LEU ILE GLN ALA ILE GLY GLU ASN LEU GLU THR PRO SER
SEQRES 4 A 479 GLY CYS ASP VAL LEU ASP GLY GLY GLY GLN TYR LEU MET
SEQRES 5 A 479 PRO GLY GLY ILE ASP PRO HIS THR HIS MET GLN LEU PRO
SEQRES 6 A 479 PHE MET GLY THR VAL ALA SER GLU ASP PHE PHE SER GLY
SEQRES 7 A 479 THR ALA ALA GLY LEU ALA GLY GLY THR THR SER ILE ILE
SEQRES 8 A 479 ASP PHE VAL ILE PRO ASN PRO ARG GLN SER LEU LEU GLU
SEQRES 9 A 479 ALA PHE HIS THR TRP ARG GLY TRP ALA GLN LYS SER ALA
SEQRES 10 A 479 ALA ASP TYR GLY PHE HIS VAL ALA ILE THR TRP TRP SER
SEQRES 11 A 479 ASP GLU VAL ALA ARG GLU MET GLY GLU LEU VAL ALA GLN
SEQRES 12 A 479 HIS GLY VAL ASN SER PHE KCX HIS PHE MET ALA TYR LYS
SEQRES 13 A 479 ASN ALA ILE MET ALA ALA ASP ASP THR LEU VAL ALA SER
SEQRES 14 A 479 PHE GLU ARG CYS LEU GLU LEU GLY ALA VAL PRO THR VAL
SEQRES 15 A 479 HIS ALA GLU ASN GLY GLU LEU VAL PHE HIS LEU GLN GLN
SEQRES 16 A 479 LYS LEU LEU ALA GLN GLY LEU THR GLY PRO GLU ALA HIS
SEQRES 17 A 479 PRO LEU SER ARG PRO PRO GLN VAL GLU GLY GLU ALA ALA
SEQRES 18 A 479 SER ARG ALA ILE ARG ILE ALA GLU THR LEU GLY THR PRO
SEQRES 19 A 479 LEU TYR LEU VAL HIS ILE SER SER ARG GLU ALA LEU ASP
SEQRES 20 A 479 GLU ILE ALA TYR ALA ARG ALA LYS GLY GLN PRO VAL TYR
SEQRES 21 A 479 GLY GLU VAL LEU ALA GLY HIS LEU LEU LEU ASP ASP SER
SEQRES 22 A 479 VAL TYR ARG HIS PRO ASP TRP ALA THR ALA ALA GLY TYR
SEQRES 23 A 479 VAL MET SER PRO PRO PHE ARG PRO VAL GLU HIS GLN GLU
SEQRES 24 A 479 ALA LEU TRP ARG GLY LEU GLN SER GLY ASN LEU HIS THR
SEQRES 25 A 479 THR ALA THR ASP HIS CYS CYS PHE CYS ALA GLU GLN LYS
SEQRES 26 A 479 ALA MET GLY ARG ASP ASP PHE SER LYS ILE PRO ASN GLY
SEQRES 27 A 479 THR ALA GLY ILE GLU ASP ARG MET ALA LEU LEU TRP ASP
SEQRES 28 A 479 ALA GLY VAL ASN SER GLY ARG LEU SER MET HIS GLU PHE
SEQRES 29 A 479 VAL ALA LEU THR SER THR ASN THR ALA LYS ILE PHE ASN
SEQRES 30 A 479 LEU PHE PRO ARG LYS GLY ALA ILE ARG VAL GLY ALA ASP
SEQRES 31 A 479 ALA ASP LEU VAL LEU TRP ASP PRO GLN GLY SER ARG THR
SEQRES 32 A 479 LEU SER ALA ALA THR HIS HIS GLN ARG VAL ASP PHE ASN
SEQRES 33 A 479 ILE PHE GLU GLY ARG THR VAL ARG GLY ILE PRO SER HIS
SEQRES 34 A 479 THR ILE SER GLN GLY LYS LEU LEU TRP ALA ALA GLY ASP
SEQRES 35 A 479 LEU ARG ALA GLU PRO GLY ALA GLY ARG TYR VAL GLU ARG
SEQRES 36 A 479 PRO ALA TYR PRO SER VAL TYR GLU VAL LEU GLY ARG ARG
SEQRES 37 A 479 ALA GLU ARG GLN ARG PRO VAL ALA VAL GLU ARG
SEQRES 1 B 479 MET SER LEU LEU ILE ARG GLY ALA THR VAL VAL THR HIS
SEQRES 2 B 479 GLU GLU SER TYR ARG ALA ASP VAL LEU CYS ALA ASN GLY
SEQRES 3 B 479 LEU ILE GLN ALA ILE GLY GLU ASN LEU GLU THR PRO SER
SEQRES 4 B 479 GLY CYS ASP VAL LEU ASP GLY GLY GLY GLN TYR LEU MET
SEQRES 5 B 479 PRO GLY GLY ILE ASP PRO HIS THR HIS MET GLN LEU PRO
SEQRES 6 B 479 PHE MET GLY THR VAL ALA SER GLU ASP PHE PHE SER GLY
SEQRES 7 B 479 THR ALA ALA GLY LEU ALA GLY GLY THR THR SER ILE ILE
SEQRES 8 B 479 ASP PHE VAL ILE PRO ASN PRO ARG GLN SER LEU LEU GLU
SEQRES 9 B 479 ALA PHE HIS THR TRP ARG GLY TRP ALA GLN LYS SER ALA
SEQRES 10 B 479 ALA ASP TYR GLY PHE HIS VAL ALA ILE THR TRP TRP SER
SEQRES 11 B 479 ASP GLU VAL ALA ARG GLU MET GLY GLU LEU VAL ALA GLN
SEQRES 12 B 479 HIS GLY VAL ASN SER PHE KCX HIS PHE MET ALA TYR LYS
SEQRES 13 B 479 ASN ALA ILE MET ALA ALA ASP ASP THR LEU VAL ALA SER
SEQRES 14 B 479 PHE GLU ARG CYS LEU GLU LEU GLY ALA VAL PRO THR VAL
SEQRES 15 B 479 HIS ALA GLU ASN GLY GLU LEU VAL PHE HIS LEU GLN GLN
SEQRES 16 B 479 LYS LEU LEU ALA GLN GLY LEU THR GLY PRO GLU ALA HIS
SEQRES 17 B 479 PRO LEU SER ARG PRO PRO GLN VAL GLU GLY GLU ALA ALA
SEQRES 18 B 479 SER ARG ALA ILE ARG ILE ALA GLU THR LEU GLY THR PRO
SEQRES 19 B 479 LEU TYR LEU VAL HIS ILE SER SER ARG GLU ALA LEU ASP
SEQRES 20 B 479 GLU ILE ALA TYR ALA ARG ALA LYS GLY GLN PRO VAL TYR
SEQRES 21 B 479 GLY GLU VAL LEU ALA GLY HIS LEU LEU LEU ASP ASP SER
SEQRES 22 B 479 VAL TYR ARG HIS PRO ASP TRP ALA THR ALA ALA GLY TYR
SEQRES 23 B 479 VAL MET SER PRO PRO PHE ARG PRO VAL GLU HIS GLN GLU
SEQRES 24 B 479 ALA LEU TRP ARG GLY LEU GLN SER GLY ASN LEU HIS THR
SEQRES 25 B 479 THR ALA THR ASP HIS CYS CYS PHE CYS ALA GLU GLN LYS
SEQRES 26 B 479 ALA MET GLY ARG ASP ASP PHE SER LYS ILE PRO ASN GLY
SEQRES 27 B 479 THR ALA GLY ILE GLU ASP ARG MET ALA LEU LEU TRP ASP
SEQRES 28 B 479 ALA GLY VAL ASN SER GLY ARG LEU SER MET HIS GLU PHE
SEQRES 29 B 479 VAL ALA LEU THR SER THR ASN THR ALA LYS ILE PHE ASN
SEQRES 30 B 479 LEU PHE PRO ARG LYS GLY ALA ILE ARG VAL GLY ALA ASP
SEQRES 31 B 479 ALA ASP LEU VAL LEU TRP ASP PRO GLN GLY SER ARG THR
SEQRES 32 B 479 LEU SER ALA ALA THR HIS HIS GLN ARG VAL ASP PHE ASN
SEQRES 33 B 479 ILE PHE GLU GLY ARG THR VAL ARG GLY ILE PRO SER HIS
SEQRES 34 B 479 THR ILE SER GLN GLY LYS LEU LEU TRP ALA ALA GLY ASP
SEQRES 35 B 479 LEU ARG ALA GLU PRO GLY ALA GLY ARG TYR VAL GLU ARG
SEQRES 36 B 479 PRO ALA TYR PRO SER VAL TYR GLU VAL LEU GLY ARG ARG
SEQRES 37 B 479 ALA GLU ARG GLN ARG PRO VAL ALA VAL GLU ARG
MODRES 6KLK KCX A 150 LYS MODIFIED RESIDUE
MODRES 6KLK KCX B 150 LYS MODIFIED RESIDUE
HET KCX A 150 12
HET KCX B 150 12
HET URF A 501 12
HET ZN A 502 1
HET ZN A 503 1
HET ZN B 501 1
HET ZN B 502 1
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM URF 5-FLUOROURACIL
HETNAM ZN ZINC ION
FORMUL 1 KCX 2(C7 H14 N2 O4)
FORMUL 3 URF C4 H3 F N2 O2
FORMUL 4 ZN 4(ZN 2+)
FORMUL 8 HOH *567(H2 O)
HELIX 1 AA1 ASP A 74 GLY A 85 1 12
HELIX 2 AA2 SER A 101 GLN A 114 1 14
HELIX 3 AA3 SER A 130 HIS A 144 1 15
HELIX 4 AA4 ALA A 162 GLY A 177 1 16
HELIX 5 AA5 ASN A 186 GLN A 200 1 15
HELIX 6 AA6 GLU A 206 SER A 211 1 6
HELIX 7 AA7 PRO A 213 GLY A 232 1 20
HELIX 8 AA8 SER A 242 ALA A 254 1 13
HELIX 9 AA9 ALA A 265 LEU A 270 1 6
HELIX 10 AB1 ASP A 271 HIS A 277 5 7
HELIX 11 AB2 ASP A 279 TYR A 286 1 8
HELIX 12 AB3 PRO A 294 SER A 307 1 14
HELIX 13 AB4 CYS A 321 ALA A 326 1 6
HELIX 14 AB5 MET A 327 ARG A 329 5 3
HELIX 15 AB6 ASP A 331 ILE A 335 5 5
HELIX 16 AB7 ASP A 344 VAL A 354 1 11
HELIX 17 AB8 SER A 360 SER A 369 1 10
HELIX 18 AB9 SER A 369 PHE A 376 1 8
HELIX 19 AC1 SER A 460 GLN A 472 1 13
HELIX 20 AC2 ASP B 74 GLY B 85 1 12
HELIX 21 AC3 SER B 101 GLN B 114 1 14
HELIX 22 AC4 SER B 130 GLY B 145 1 16
HELIX 23 AC5 ALA B 162 GLY B 177 1 16
HELIX 24 AC6 ASN B 186 GLN B 200 1 15
HELIX 25 AC7 GLU B 206 SER B 211 1 6
HELIX 26 AC8 PRO B 213 GLY B 232 1 20
HELIX 27 AC9 SER B 242 ALA B 254 1 13
HELIX 28 AD1 ALA B 265 LEU B 270 1 6
HELIX 29 AD2 ASP B 271 HIS B 277 5 7
HELIX 30 AD3 ASP B 279 TYR B 286 1 8
HELIX 31 AD4 PRO B 294 SER B 307 1 14
HELIX 32 AD5 CYS B 321 ALA B 326 1 6
HELIX 33 AD6 MET B 327 ARG B 329 5 3
HELIX 34 AD7 ASP B 331 ILE B 335 5 5
HELIX 35 AD8 ASP B 344 VAL B 354 1 11
HELIX 36 AD9 SER B 360 SER B 369 1 10
HELIX 37 AE1 SER B 369 PHE B 376 1 8
HELIX 38 AE2 SER B 460 GLN B 472 1 13
SHEET 1 AA1 4 LEU A 27 GLY A 32 0
SHEET 2 AA1 4 ASP A 20 ALA A 24 -1 N LEU A 22 O GLN A 29
SHEET 3 AA1 4 LEU A 3 ARG A 6 -1 N LEU A 3 O CYS A 23
SHEET 4 AA1 4 ASP A 42 ASP A 45 1 O LEU A 44 N LEU A 4
SHEET 1 AA2 7 SER A 16 ARG A 18 0
SHEET 2 AA2 7 THR A 9 VAL A 11 -1 N VAL A 10 O TYR A 17
SHEET 3 AA2 7 TYR A 50 PRO A 53 1 O LEU A 51 N VAL A 11
SHEET 4 AA2 7 LEU A 393 THR A 403 -1 O TRP A 396 N TYR A 50
SHEET 5 AA2 7 THR A 422 SER A 432 -1 O ILE A 431 N LEU A 393
SHEET 6 AA2 7 LYS A 435 ALA A 439 -1 O LYS A 435 N SER A 432
SHEET 7 AA2 7 ASP A 442 LEU A 443 -1 O ASP A 442 N ALA A 439
SHEET 1 AA3 8 GLY A 55 ASP A 57 0
SHEET 2 AA3 8 THR A 87 VAL A 94 1 O SER A 89 N ASP A 57
SHEET 3 AA3 8 ASP A 119 ALA A 125 1 O ALA A 125 N VAL A 94
SHEET 4 AA3 8 SER A 148 PHE A 152 1 O KCX A 150 N VAL A 124
SHEET 5 AA3 8 VAL A 179 HIS A 183 1 O HIS A 183 N HIS A 151
SHEET 6 AA3 8 LEU A 235 LEU A 237 1 O TYR A 236 N PRO A 180
SHEET 7 AA3 8 VAL A 259 LEU A 264 1 O TYR A 260 N LEU A 235
SHEET 8 AA3 8 THR A 312 ALA A 314 1 O THR A 312 N VAL A 263
SHEET 1 AA4 2 PRO A 65 PHE A 66 0
SHEET 2 AA4 2 THR A 69 VAL A 70 -1 O THR A 69 N PHE A 66
SHEET 1 AA5 4 LEU B 27 GLY B 32 0
SHEET 2 AA5 4 ASP B 20 ALA B 24 -1 N LEU B 22 O GLN B 29
SHEET 3 AA5 4 LEU B 3 ARG B 6 -1 N ILE B 5 O VAL B 21
SHEET 4 AA5 4 ASP B 42 ASP B 45 1 O ASP B 42 N LEU B 4
SHEET 1 AA6 7 SER B 16 ARG B 18 0
SHEET 2 AA6 7 THR B 9 VAL B 11 -1 N VAL B 10 O TYR B 17
SHEET 3 AA6 7 TYR B 50 PRO B 53 1 O LEU B 51 N THR B 9
SHEET 4 AA6 7 LEU B 393 THR B 403 -1 O TRP B 396 N TYR B 50
SHEET 5 AA6 7 THR B 422 SER B 432 -1 O ILE B 431 N LEU B 393
SHEET 6 AA6 7 LYS B 435 ALA B 439 -1 O LYS B 435 N SER B 432
SHEET 7 AA6 7 ASP B 442 LEU B 443 -1 O ASP B 442 N ALA B 439
SHEET 1 AA7 8 GLY B 55 ASP B 57 0
SHEET 2 AA7 8 THR B 87 VAL B 94 1 O SER B 89 N ASP B 57
SHEET 3 AA7 8 ASP B 119 ALA B 125 1 O ALA B 125 N VAL B 94
SHEET 4 AA7 8 SER B 148 PHE B 152 1 O SER B 148 N VAL B 124
SHEET 5 AA7 8 VAL B 179 HIS B 183 1 O HIS B 183 N HIS B 151
SHEET 6 AA7 8 LEU B 235 LEU B 237 1 O TYR B 236 N PRO B 180
SHEET 7 AA7 8 VAL B 259 LEU B 264 1 O TYR B 260 N LEU B 237
SHEET 8 AA7 8 THR B 312 ALA B 314 1 O THR B 312 N VAL B 263
SHEET 1 AA8 2 PRO B 65 PHE B 66 0
SHEET 2 AA8 2 THR B 69 VAL B 70 -1 O THR B 69 N PHE B 66
LINK C PHE A 149 N KCX A 150 1555 1555 1.33
LINK C KCX A 150 N HIS A 151 1555 1555 1.33
LINK C PHE B 149 N KCX B 150 1555 1555 1.33
LINK C KCX B 150 N HIS B 151 1555 1555 1.33
LINK NE2 HIS A 59 ZN ZN A 502 1555 1555 2.11
LINK NE2 HIS A 61 ZN ZN A 502 1555 1555 2.10
LINK OQ2 KCX A 150 ZN ZN A 502 1555 1555 2.11
LINK OQ1 KCX A 150 ZN ZN A 503 1555 1555 1.96
LINK ND1 HIS A 183 ZN ZN A 503 1555 1555 2.12
LINK OD1 ASP A 316 ZN ZN A 502 1555 1555 2.15
LINK NE2 HIS B 59 ZN ZN B 501 1555 1555 2.09
LINK NE2 HIS B 61 ZN ZN B 501 1555 1555 2.15
LINK OQ2 KCX B 150 ZN ZN B 501 1555 1555 2.01
LINK OQ1 KCX B 150 ZN ZN B 502 1555 1555 1.86
LINK ND1 HIS B 183 ZN ZN B 502 1555 1555 2.32
LINK OD1 ASP B 316 ZN ZN B 501 1555 1555 2.07
CISPEP 1 SER A 289 PRO A 290 0 1.83
CISPEP 2 PHE A 379 PRO A 380 0 8.73
CISPEP 3 SER B 289 PRO B 290 0 4.00
CISPEP 4 PHE B 379 PRO B 380 0 7.55
SITE 1 AC1 12 HIS A 61 LEU A 64 KCX A 150 PHE A 152
SITE 2 AC1 12 TYR A 155 MET A 288 SER A 289 ASP A 316
SITE 3 AC1 12 CYS A 318 ASN A 337 ZN A 502 ZN A 503
SITE 1 AC2 6 HIS A 59 HIS A 61 KCX A 150 ASP A 316
SITE 2 AC2 6 URF A 501 ZN A 503
SITE 1 AC3 5 KCX A 150 HIS A 183 HIS A 239 URF A 501
SITE 2 AC3 5 ZN A 502
SITE 1 AC4 5 HIS B 59 HIS B 61 KCX B 150 ASP B 316
SITE 2 AC4 5 ZN B 502
SITE 1 AC5 4 KCX B 150 HIS B 183 HIS B 239 ZN B 501
CRYST1 111.333 111.333 159.977 90.00 90.00 120.00 P 31 2 1 12
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 0.008982 0.005186 0.000000 0.00000
SCALE2 0.000000 0.010372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006251 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
