HEADER HYDROLASE 08-OCT-15 5E5C
TITLE CRYSTAL STRUCTURE OF DIHYDROPYRIMIDINASE FROM PSEUDOMONAS AERUGINOSA
TITLE 2 PAO1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-HYDANTOINASE/DIHYDROPYRIMIDINASE;
COMPND 3 CHAIN: A, C;
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 /
SOURCE 3 PAO1 / 1C / PRS 101 / LMG 12228);
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 6 GENE: DHT, PA0441;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DIHYDROPYRIMIDINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.C.HUANG,Y.H.HUANG,Y.C.HSIEH,C.T.TZENG,C.J.CHEN,C.Y.HUANG
REVDAT 4 15-NOV-23 5E5C 1 REMARK
REVDAT 3 08-NOV-23 5E5C 1 JRNL REMARK LINK
REVDAT 2 28-SEP-16 5E5C 1 JRNL
REVDAT 1 21-SEP-16 5E5C 0
JRNL AUTH C.T.TZENG,Y.H.HUANG,C.Y.HUANG
JRNL TITL CRYSTAL STRUCTURE OF DIHYDROPYRIMIDINASE FROM PSEUDOMONAS
JRNL TITL 2 AERUGINOSA PAO1: INSIGHTS INTO THE MOLECULAR BASIS OF
JRNL TITL 3 FORMATION OF A DIMER
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 478 1449 2016
JRNL REFN ESSN 1090-2104
JRNL PMID 27576201
JRNL DOI 10.1016/J.BBRC.2016.08.144
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 97.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 65158
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3471
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4716
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 230
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7356
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 338
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.11000
REMARK 3 B12 (A**2) : -0.02000
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): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.158
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.515
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7540 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7029 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10254 ; 1.879 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16115 ; 0.900 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 955 ; 6.430 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 350 ;34.995 ;23.086
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1147 ;14.662 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 62 ;18.921 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1113 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8719 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1819 ; 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): 3826 ; 2.446 ; 2.741
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3825 ; 2.442 ; 2.740
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4779 ; 3.383 ; 4.102
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4780 ; 3.383 ; 4.103
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3714 ; 3.409 ; 3.117
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3715 ; 3.408 ; 3.117
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5476 ; 5.103 ; 4.535
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8899 ; 6.344 ;22.644
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8778 ; 6.325 ;22.573
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 5E5C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000213679.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68799
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 97.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.976
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: 2FTW
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG8000, 100MM HEPES SODIUM SALT,
REMARK 280 200MM CALCIUM ACETATE, PH 7.5, EVAPORATION, 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 53.68333
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 107.36667
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 107.36667
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 53.68333
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -327.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 465 HIS A 480
REMARK 465 HIS A 481
REMARK 465 HIS A 482
REMARK 465 HIS A 483
REMARK 465 HIS A 484
REMARK 465 HIS A 485
REMARK 465 HIS C 480
REMARK 465 HIS C 481
REMARK 465 HIS C 482
REMARK 465 HIS C 483
REMARK 465 HIS C 484
REMARK 465 HIS C 485
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 OE1 GLU C 188 O HOH C 601 2.03
REMARK 500 NH2 ARG A 467 O HOH A 601 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 460 CB SER A 460 OG -0.083
REMARK 500 SER C 369 CA SER C 369 CB 0.101
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 ASP A 74 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP A 74 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 172 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 412 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 412 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 SER A 460 N - CA - CB ANGL. DEV. = -10.0 DEGREES
REMARK 500 ARG A 467 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 467 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 468 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 223 NE - CZ - NH1 ANGL. DEV. = -3.3 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 12 -167.25 -106.31
REMARK 500 GLU A 14 -6.76 -146.95
REMARK 500 GLN A 63 41.09 34.44
REMARK 500 ARG A 99 -4.40 68.95
REMARK 500 ALA A 154 -162.84 -107.99
REMARK 500 ALA A 158 -105.47 -151.44
REMARK 500 HIS A 239 81.93 8.90
REMARK 500 CYS A 318 86.43 -153.81
REMARK 500 ASP A 331 100.06 -167.19
REMARK 500 SER A 369 -50.42 -142.84
REMARK 500 ALA A 440 65.33 39.51
REMARK 500 GLU C 14 -12.51 -148.13
REMARK 500 ARG C 99 -3.44 68.58
REMARK 500 LYS C 115 4.08 -69.88
REMARK 500 ALA C 154 -165.66 -113.27
REMARK 500 ASN C 157 10.83 55.70
REMARK 500 ALA C 158 -89.75 -120.17
REMARK 500 ARG C 212 69.71 -155.31
REMARK 500 HIS C 239 69.29 19.31
REMARK 500 CYS C 318 88.10 -151.77
REMARK 500 ASP C 331 105.10 -174.43
REMARK 500 SER C 369 -49.49 -153.69
REMARK 500 GLN C 433 54.77 39.74
REMARK 500 ALA C 440 58.15 33.25
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 94.1
REMARK 620 3 KCX A 150 OQ1 83.3 88.2
REMARK 620 4 ASP A 316 OD1 87.1 84.7 167.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 150 OQ2
REMARK 620 2 HIS A 183 ND1 92.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 59 NE2
REMARK 620 2 HIS C 61 NE2 95.9
REMARK 620 3 KCX C 150 OQ1 84.7 79.7
REMARK 620 4 ASP C 316 OD1 88.0 92.7 168.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN 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 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 502
DBREF 5E5C A 1 479 UNP Q9I676 HYDA_PSEAE 1 479
DBREF 5E5C C 1 479 UNP Q9I676 HYDA_PSEAE 1 479
SEQADV 5E5C HIS A 480 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS A 481 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS A 482 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS A 483 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS A 484 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS A 485 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS C 480 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS C 481 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS C 482 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS C 483 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS C 484 UNP Q9I676 EXPRESSION TAG
SEQADV 5E5C HIS C 485 UNP Q9I676 EXPRESSION TAG
SEQRES 1 A 485 MET SER LEU LEU ILE ARG GLY ALA THR VAL VAL THR HIS
SEQRES 2 A 485 GLU GLU SER TYR ARG ALA ASP VAL LEU CYS ALA ASN GLY
SEQRES 3 A 485 LEU ILE GLN ALA ILE GLY GLU ASN LEU GLU THR PRO SER
SEQRES 4 A 485 GLY CYS ASP VAL LEU ASP GLY GLY GLY GLN TYR LEU MET
SEQRES 5 A 485 PRO GLY GLY ILE ASP PRO HIS THR HIS MET GLN LEU PRO
SEQRES 6 A 485 PHE MET GLY THR VAL ALA SER GLU ASP PHE PHE SER GLY
SEQRES 7 A 485 THR ALA ALA GLY LEU ALA GLY GLY THR THR SER ILE ILE
SEQRES 8 A 485 ASP PHE VAL ILE PRO ASN PRO ARG GLN SER LEU LEU GLU
SEQRES 9 A 485 ALA PHE HIS THR TRP ARG GLY TRP ALA GLN LYS SER ALA
SEQRES 10 A 485 ALA ASP TYR GLY PHE HIS VAL ALA ILE THR TRP TRP SER
SEQRES 11 A 485 ASP GLU VAL ALA ARG GLU MET GLY GLU LEU VAL ALA GLN
SEQRES 12 A 485 HIS GLY VAL ASN SER PHE KCX HIS PHE MET ALA TYR LYS
SEQRES 13 A 485 ASN ALA ILE MET ALA ALA ASP ASP THR LEU VAL ALA SER
SEQRES 14 A 485 PHE GLU ARG CYS LEU GLU LEU GLY ALA VAL PRO THR VAL
SEQRES 15 A 485 HIS ALA GLU ASN GLY GLU LEU VAL PHE HIS LEU GLN GLN
SEQRES 16 A 485 LYS LEU LEU ALA GLN GLY LEU THR GLY PRO GLU ALA HIS
SEQRES 17 A 485 PRO LEU SER ARG PRO PRO GLN VAL GLU GLY GLU ALA ALA
SEQRES 18 A 485 SER ARG ALA ILE ARG ILE ALA GLU THR LEU GLY THR PRO
SEQRES 19 A 485 LEU TYR LEU VAL HIS ILE SER SER ARG GLU ALA LEU ASP
SEQRES 20 A 485 GLU ILE ALA TYR ALA ARG ALA LYS GLY GLN PRO VAL TYR
SEQRES 21 A 485 GLY GLU VAL LEU ALA GLY HIS LEU LEU LEU ASP ASP SER
SEQRES 22 A 485 VAL TYR ARG HIS PRO ASP TRP ALA THR ALA ALA GLY TYR
SEQRES 23 A 485 VAL MET SER PRO PRO PHE ARG PRO VAL GLU HIS GLN GLU
SEQRES 24 A 485 ALA LEU TRP ARG GLY LEU GLN SER GLY ASN LEU HIS THR
SEQRES 25 A 485 THR ALA THR ASP HIS CYS CYS PHE CYS ALA GLU GLN LYS
SEQRES 26 A 485 ALA MET GLY ARG ASP ASP PHE SER LYS ILE PRO ASN GLY
SEQRES 27 A 485 THR ALA GLY ILE GLU ASP ARG MET ALA LEU LEU TRP ASP
SEQRES 28 A 485 ALA GLY VAL ASN SER GLY ARG LEU SER MET HIS GLU PHE
SEQRES 29 A 485 VAL ALA LEU THR SER THR ASN THR ALA LYS ILE PHE ASN
SEQRES 30 A 485 LEU PHE PRO ARG LYS GLY ALA ILE ARG VAL GLY ALA ASP
SEQRES 31 A 485 ALA ASP LEU VAL LEU TRP ASP PRO GLN GLY SER ARG THR
SEQRES 32 A 485 LEU SER ALA ALA THR HIS HIS GLN ARG VAL ASP PHE ASN
SEQRES 33 A 485 ILE PHE GLU GLY ARG THR VAL ARG GLY ILE PRO SER HIS
SEQRES 34 A 485 THR ILE SER GLN GLY LYS LEU LEU TRP ALA ALA GLY ASP
SEQRES 35 A 485 LEU ARG ALA GLU PRO GLY ALA GLY ARG TYR VAL GLU ARG
SEQRES 36 A 485 PRO ALA TYR PRO SER VAL TYR GLU VAL LEU GLY ARG ARG
SEQRES 37 A 485 ALA GLU ARG GLN ARG PRO VAL ALA VAL GLU ARG HIS HIS
SEQRES 38 A 485 HIS HIS HIS HIS
SEQRES 1 C 485 MET SER LEU LEU ILE ARG GLY ALA THR VAL VAL THR HIS
SEQRES 2 C 485 GLU GLU SER TYR ARG ALA ASP VAL LEU CYS ALA ASN GLY
SEQRES 3 C 485 LEU ILE GLN ALA ILE GLY GLU ASN LEU GLU THR PRO SER
SEQRES 4 C 485 GLY CYS ASP VAL LEU ASP GLY GLY GLY GLN TYR LEU MET
SEQRES 5 C 485 PRO GLY GLY ILE ASP PRO HIS THR HIS MET GLN LEU PRO
SEQRES 6 C 485 PHE MET GLY THR VAL ALA SER GLU ASP PHE PHE SER GLY
SEQRES 7 C 485 THR ALA ALA GLY LEU ALA GLY GLY THR THR SER ILE ILE
SEQRES 8 C 485 ASP PHE VAL ILE PRO ASN PRO ARG GLN SER LEU LEU GLU
SEQRES 9 C 485 ALA PHE HIS THR TRP ARG GLY TRP ALA GLN LYS SER ALA
SEQRES 10 C 485 ALA ASP TYR GLY PHE HIS VAL ALA ILE THR TRP TRP SER
SEQRES 11 C 485 ASP GLU VAL ALA ARG GLU MET GLY GLU LEU VAL ALA GLN
SEQRES 12 C 485 HIS GLY VAL ASN SER PHE KCX HIS PHE MET ALA TYR LYS
SEQRES 13 C 485 ASN ALA ILE MET ALA ALA ASP ASP THR LEU VAL ALA SER
SEQRES 14 C 485 PHE GLU ARG CYS LEU GLU LEU GLY ALA VAL PRO THR VAL
SEQRES 15 C 485 HIS ALA GLU ASN GLY GLU LEU VAL PHE HIS LEU GLN GLN
SEQRES 16 C 485 LYS LEU LEU ALA GLN GLY LEU THR GLY PRO GLU ALA HIS
SEQRES 17 C 485 PRO LEU SER ARG PRO PRO GLN VAL GLU GLY GLU ALA ALA
SEQRES 18 C 485 SER ARG ALA ILE ARG ILE ALA GLU THR LEU GLY THR PRO
SEQRES 19 C 485 LEU TYR LEU VAL HIS ILE SER SER ARG GLU ALA LEU ASP
SEQRES 20 C 485 GLU ILE ALA TYR ALA ARG ALA LYS GLY GLN PRO VAL TYR
SEQRES 21 C 485 GLY GLU VAL LEU ALA GLY HIS LEU LEU LEU ASP ASP SER
SEQRES 22 C 485 VAL TYR ARG HIS PRO ASP TRP ALA THR ALA ALA GLY TYR
SEQRES 23 C 485 VAL MET SER PRO PRO PHE ARG PRO VAL GLU HIS GLN GLU
SEQRES 24 C 485 ALA LEU TRP ARG GLY LEU GLN SER GLY ASN LEU HIS THR
SEQRES 25 C 485 THR ALA THR ASP HIS CYS CYS PHE CYS ALA GLU GLN LYS
SEQRES 26 C 485 ALA MET GLY ARG ASP ASP PHE SER LYS ILE PRO ASN GLY
SEQRES 27 C 485 THR ALA GLY ILE GLU ASP ARG MET ALA LEU LEU TRP ASP
SEQRES 28 C 485 ALA GLY VAL ASN SER GLY ARG LEU SER MET HIS GLU PHE
SEQRES 29 C 485 VAL ALA LEU THR SER THR ASN THR ALA LYS ILE PHE ASN
SEQRES 30 C 485 LEU PHE PRO ARG LYS GLY ALA ILE ARG VAL GLY ALA ASP
SEQRES 31 C 485 ALA ASP LEU VAL LEU TRP ASP PRO GLN GLY SER ARG THR
SEQRES 32 C 485 LEU SER ALA ALA THR HIS HIS GLN ARG VAL ASP PHE ASN
SEQRES 33 C 485 ILE PHE GLU GLY ARG THR VAL ARG GLY ILE PRO SER HIS
SEQRES 34 C 485 THR ILE SER GLN GLY LYS LEU LEU TRP ALA ALA GLY ASP
SEQRES 35 C 485 LEU ARG ALA GLU PRO GLY ALA GLY ARG TYR VAL GLU ARG
SEQRES 36 C 485 PRO ALA TYR PRO SER VAL TYR GLU VAL LEU GLY ARG ARG
SEQRES 37 C 485 ALA GLU ARG GLN ARG PRO VAL ALA VAL GLU ARG HIS HIS
SEQRES 38 C 485 HIS HIS HIS HIS
MODRES 5E5C KCX A 150 LYS MODIFIED RESIDUE
MODRES 5E5C KCX C 150 LYS MODIFIED RESIDUE
HET KCX A 150 12
HET KCX C 150 12
HET ZN A 501 1
HET ZN A 502 1
HET ZN C 501 1
HET ZN C 502 1
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM ZN ZINC ION
FORMUL 1 KCX 2(C7 H14 N2 O4)
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 HOH *338(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 GLY A 145 1 16
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 ARG A 212 1 7
HELIX 7 AA7 PRO A 213 GLY A 232 1 20
HELIX 8 AA8 SER A 242 LYS A 255 1 14
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 C 74 GLY C 85 1 12
HELIX 21 AC3 SER C 101 GLN C 114 1 14
HELIX 22 AC4 SER C 130 GLY C 145 1 16
HELIX 23 AC5 ALA C 162 GLY C 177 1 16
HELIX 24 AC6 ASN C 186 GLN C 200 1 15
HELIX 25 AC7 GLU C 206 SER C 211 1 6
HELIX 26 AC8 PRO C 213 GLY C 232 1 20
HELIX 27 AC9 SER C 242 LYS C 255 1 14
HELIX 28 AD1 ALA C 265 LEU C 270 1 6
HELIX 29 AD2 ASP C 271 HIS C 277 5 7
HELIX 30 AD3 ASP C 279 TYR C 286 1 8
HELIX 31 AD4 VAL C 295 SER C 307 1 13
HELIX 32 AD5 CYS C 321 ALA C 326 1 6
HELIX 33 AD6 MET C 327 ARG C 329 5 3
HELIX 34 AD7 ASP C 331 ILE C 335 5 5
HELIX 35 AD8 ASP C 344 VAL C 354 1 11
HELIX 36 AD9 SER C 360 SER C 369 1 10
HELIX 37 AE1 SER C 369 PHE C 376 1 8
HELIX 38 AE2 SER C 460 GLN C 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 ILE A 5 O VAL A 21
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 THR A 9
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 VAL A 423 N ARG A 402
SHEET 6 AA2 7 LYS A 435 ALA A 439 -1 O LEU A 437 N THR A 430
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 SER A 148 N VAL A 124
SHEET 5 AA3 8 VAL A 179 HIS A 183 1 O THR A 181 N PHE A 149
SHEET 6 AA3 8 LEU A 235 LEU A 237 1 O TYR A 236 N VAL A 182
SHEET 7 AA3 8 VAL A 259 LEU A 264 1 O TYR A 260 N LEU A 237
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 C 27 GLY C 32 0
SHEET 2 AA5 4 ASP C 20 ALA C 24 -1 N LEU C 22 O ALA C 30
SHEET 3 AA5 4 LEU C 3 ARG C 6 -1 N LEU C 3 O CYS C 23
SHEET 4 AA5 4 ASP C 42 ASP C 45 1 O LEU C 44 N ARG C 6
SHEET 1 AA6 7 SER C 16 ARG C 18 0
SHEET 2 AA6 7 THR C 9 VAL C 11 -1 N VAL C 10 O TYR C 17
SHEET 3 AA6 7 TYR C 50 PRO C 53 1 O LEU C 51 N THR C 9
SHEET 4 AA6 7 LEU C 393 THR C 403 -1 O TRP C 396 N TYR C 50
SHEET 5 AA6 7 THR C 422 SER C 432 -1 O ILE C 431 N LEU C 393
SHEET 6 AA6 7 LYS C 435 ALA C 439 -1 O LEU C 437 N THR C 430
SHEET 7 AA6 7 ASP C 442 LEU C 443 -1 O ASP C 442 N ALA C 439
SHEET 1 AA7 8 GLY C 55 THR C 60 0
SHEET 2 AA7 8 THR C 87 VAL C 94 1 O SER C 89 N ASP C 57
SHEET 3 AA7 8 ASP C 119 ALA C 125 1 O ALA C 125 N VAL C 94
SHEET 4 AA7 8 SER C 148 PHE C 152 1 O SER C 148 N VAL C 124
SHEET 5 AA7 8 VAL C 179 HIS C 183 1 O THR C 181 N PHE C 149
SHEET 6 AA7 8 LEU C 235 LEU C 237 1 O TYR C 236 N PRO C 180
SHEET 7 AA7 8 VAL C 259 LEU C 264 1 O TYR C 260 N LEU C 237
SHEET 8 AA7 8 THR C 312 ALA C 314 1 O THR C 312 N VAL C 263
SHEET 1 AA8 2 PRO C 65 PHE C 66 0
SHEET 2 AA8 2 THR C 69 VAL C 70 -1 O THR C 69 N PHE C 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 1.35
LINK C PHE C 149 N KCX C 150 1555 1555 1.33
LINK C KCX C 150 N HIS C 151 1555 1555 1.35
LINK NE2 HIS A 59 ZN ZN A 502 1555 1555 2.19
LINK NE2 HIS A 61 ZN ZN A 502 1555 1555 2.30
LINK OQ2 KCX A 150 ZN ZN A 501 1555 1555 1.85
LINK OQ1 KCX A 150 ZN ZN A 502 1555 1555 2.04
LINK ND1 HIS A 183 ZN ZN A 501 1555 1555 2.34
LINK OD1 ASP A 316 ZN ZN A 502 1555 1555 2.30
LINK NE2 HIS C 59 ZN ZN C 502 1555 1555 2.13
LINK NE2 HIS C 61 ZN ZN C 502 1555 1555 2.30
LINK OQ2 KCX C 150 ZN ZN C 501 1555 1555 1.94
LINK OQ1 KCX C 150 ZN ZN C 502 1555 1555 2.17
LINK OD1 ASP C 316 ZN ZN C 502 1555 1555 2.21
CISPEP 1 SER A 289 PRO A 290 0 4.12
CISPEP 2 PHE A 379 PRO A 380 0 4.49
CISPEP 3 MET C 1 SER C 2 0 -16.25
CISPEP 4 SER C 289 PRO C 290 0 5.98
CISPEP 5 PHE C 379 PRO C 380 0 6.70
SITE 1 AC1 4 KCX A 150 HIS A 183 HIS A 239 ZN A 502
SITE 1 AC2 5 HIS A 59 HIS A 61 KCX A 150 ASP A 316
SITE 2 AC2 5 ZN A 501
SITE 1 AC3 4 KCX C 150 HIS C 183 HIS C 239 ZN C 502
SITE 1 AC4 5 HIS C 59 HIS C 61 KCX C 150 ASP C 316
SITE 2 AC4 5 ZN C 501
CRYST1 112.134 112.134 161.050 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 0.008918 0.005149 0.000000 0.00000
SCALE2 0.000000 0.010298 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006209 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
