HEADER HYDROLASE 23-APR-97 1FWA
TITLE KLEBSIELLA AEROGENES UREASE, C319A VARIANT AT PH 7.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UREASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UREA AMIDOHYDROLASE;
COMPND 5 EC: 3.5.1.5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: PH 7.5;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: UREASE;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: UREA AMIDOHYDROLASE;
COMPND 13 EC: 3.5.1.5;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES;
COMPND 16 OTHER_DETAILS: PH 7.5;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: UREASE;
COMPND 19 CHAIN: C;
COMPND 20 SYNONYM: UREA AMIDOHYDROLASE;
COMPND 21 EC: 3.5.1.5;
COMPND 22 ENGINEERED: YES;
COMPND 23 MUTATION: YES;
COMPND 24 OTHER_DETAILS: PH 7.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA AEROGENES;
SOURCE 3 ORGANISM_TAXID: 28451;
SOURCE 4 GENE: UREA UREB UREC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKAU17;
SOURCE 9 EXPRESSION_SYSTEM_GENE: UREA, UREB, UREC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: KLEBSIELLA AEROGENES;
SOURCE 12 ORGANISM_TAXID: 28451;
SOURCE 13 GENE: UREA UREB UREC;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: DH5;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PKAU17;
SOURCE 18 EXPRESSION_SYSTEM_GENE: UREA, UREB, UREC;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: KLEBSIELLA AEROGENES;
SOURCE 21 ORGANISM_TAXID: 28451;
SOURCE 22 GENE: UREA UREB UREC;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: DH5;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PKAU17;
SOURCE 27 EXPRESSION_SYSTEM_GENE: UREA, UREB, UREC
KEYWDS HYDROLASE(UREA AMIDO), MUTANT, NICKEL METALLOENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.PEARSON,P.A.KARPLUS
REVDAT 4 03-NOV-21 1FWA 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1FWA 1 VERSN
REVDAT 2 24-FEB-09 1FWA 1 VERSN
REVDAT 1 15-OCT-97 1FWA 0
JRNL AUTH M.A.PEARSON,L.O.MICHEL,R.P.HAUSINGER,P.A.KARPLUS
JRNL TITL STRUCTURES OF CYS319 VARIANTS AND ACETOHYDROXAMATE-INHIBITED
JRNL TITL 2 KLEBSIELLA AEROGENES UREASE.
JRNL REF BIOCHEMISTRY V. 36 8164 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9201965
JRNL DOI 10.1021/BI970514J
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.JABRI,P.A.KARPLUS
REMARK 1 TITL STRUCTURES OF THE KLEBSIELLA AEROGENES UREASE APOENZYME AND
REMARK 1 TITL 2 TWO ACTIVE-SITE MUTANTS
REMARK 1 REF BIOCHEMISTRY V. 35 10616 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.JABRI,M.B.CARR,R.P.HAUSINGER,P.A.KARPLUS
REMARK 1 TITL THE CRYSTAL STRUCTURE OF UREASE FROM KLEBSIELLA AEROGENES
REMARK 1 REF SCIENCE V. 268 998 1995
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.R.MARTIN,R.P.HAUSINGER
REMARK 1 TITL SITE-DIRECTED MUTAGENESIS OF THE ACTIVE SITE CYSTEINE IN
REMARK 1 TITL 2 KLEBSIELLA AEROGENES UREASE
REMARK 1 REF J.BIOL.CHEM. V. 267 20024 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.J.TODD,R.P.HAUSINGER
REMARK 1 TITL IDENTIFICATION OF THE ESSENTIAL CYSTEINE RESIDUE IN
REMARK 1 TITL 2 KLEBSIELLA AEROGENES UREASE
REMARK 1 REF J.BIOL.CHEM. V. 266 24327 1991
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 51039
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5788
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 281
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.481
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE OCCUPANCIES FOR ACTIVE SITE WATERS HOH 500 - HOH 502
REMARK 3 WERE REFINED WITH A FIXED B-FACTOR OF 20 ANGSTROMS**2.
REMARK 3 THE REFINED OCCUPANCIES FOR THESE WATERS SUGGEST NEARLY
REMARK 3 FULL OCCUPANCY FOR EACH OF THEM, ALTHOUGH THEY ARE
REMARK 3 POSITIONED TOO CLOSE (~ 2.0 ANGSTROMS APART) FOR
REMARK 3 SIMULTANEOUS OCCUPANCY.
REMARK 4
REMARK 4 1FWA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173442.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51384
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 85.40000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 85.40000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 85.40000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 85.40000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 85.40000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 85.40000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 85.40000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 85.40000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 85.40000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 85.40000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 85.40000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 85.40000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 85.40000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 85.40000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 85.40000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 85.40000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 85.40000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 85.40000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 85.40000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 85.40000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 85.40000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 85.40000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 85.40000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: NONAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 48750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -323.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THIS MODEL IS THAT OF THE C319A MUTANT (PH=7.5) AT 2.0
REMARK 400 ANGSTROMS. THE ACTIVE SITE IS NEARLY IDENTICAL TO
REMARK 400 THAT OF THE HOLOENZYME (PDB ENTRY 1KAU).
REMARK 400 THREE NONIDENTICAL CHAINS, GAMMA (A), BETA (B), AND ALPHA
REMARK 400 (C) FORM ONE (ABC)-UNIT. THE ASYMMETRIC UNIT CONTAINS ONE
REMARK 400 (ABC)-UNIT.
REMARK 400 RESIDUES 312 - 336 IN CHAIN C, THE MOBILE ACTIVE SITE FLAP,
REMARK 400 ARE MORE WELL ORDERED THAN IN THE HOLOENZYME (1KAU).
REMARK 400 THREE WATERS, 500, 501, AND 502 (FORMERLY WAT-1) ARE
REMARK 400 LIGATED TO THE ACTIVE SITE NICKEL IONS. THEY MUST BE
REMARK 400 PARTIALLY OCCUPIED DUE TO CLOSE OXYGEN-OXYGEN DISTANCES
REMARK 400 BETWEEN THEM.
REMARK 400 A TEST REFINEMENT WAS CARRIED OUT WITH CARBONATE ION IN
REMARK 400 PLACE OF WATERS 500, 501, AND 502, RESULTING IN AN
REMARK 400 R-FACTOR OF 17.0%, BUT POOR GEOMETRY FOR THE
REMARK 400 CARBONATE-METAL INTERACTIONS. THE COORDINATES FOR THE
REMARK 400 CARBONATE ARE INCLUDED FOLLOWING CHAIN C, WITH
REMARK 400 AN OCCUPANCY OF ZERO.
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 GLU B 102
REMARK 465 VAL B 103
REMARK 465 ASN B 104
REMARK 465 ASP B 105
REMARK 465 GLU B 106
REMARK 465 MET C 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 O3 CO3 C 999 O HOH C 1230 0.27
REMARK 500 C CO3 C 999 O HOH C 1230 1.10
REMARK 500 O1 CO3 C 999 O HOH C 1230 2.02
REMARK 500 O2 CO3 C 999 O HOH C 1230 2.17
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 PRO C 174 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASN C 299 N - CA - C ANGL. DEV. = 17.1 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 ALA B 85 -145.93 -123.01
REMARK 500 PHE B 93 -121.47 58.82
REMARK 500 ALA C 24 -131.28 53.69
REMARK 500 LYS C 49 -154.61 -90.06
REMARK 500 MET C 55 -106.71 -100.92
REMARK 500 PRO C 188 28.93 -75.40
REMARK 500 HIS C 272 61.23 30.22
REMARK 500 HIS C 280 119.27 -37.13
REMARK 500 SER C 359 -63.54 -94.21
REMARK 500 ASP C 360 45.68 86.45
REMARK 500 ALA C 363 51.70 -146.88
REMARK 500 MET C 364 48.09 87.57
REMARK 500 THR C 408 -88.51 -126.38
REMARK 500 ALA C 561 -111.07 -127.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 CO3 C 999
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 NI C 575 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 134 NE2
REMARK 620 2 HIS C 136 NE2 120.4
REMARK 620 3 KCX C 217 OQ2 90.0 96.3
REMARK 620 4 ASP C 360 OD1 84.0 86.8 174.0
REMARK 620 5 CO3 C 999 O1 94.7 144.1 90.3 90.1
REMARK 620 6 CO3 C 999 O3 153.0 81.0 104.5 81.0 63.2
REMARK 620 7 HOH C1228 O 101.9 137.4 87.1 94.0 7.9 57.3
REMARK 620 8 HOH C1230 O 149.2 86.1 103.2 82.1 58.1 5.1 52.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 574 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 217 OQ1
REMARK 620 2 HIS C 246 ND1 94.6
REMARK 620 3 HIS C 272 NE2 108.3 97.7
REMARK 620 4 CO3 C 999 O1 92.7 150.9 106.6
REMARK 620 5 CO3 C 999 O2 100.3 89.2 149.8 61.7
REMARK 620 6 HOH C1228 O 93.6 143.3 113.3 7.6 54.1
REMARK 620 7 HOH C1229 O 98.9 89.7 151.0 61.3 1.4 53.8
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NIL
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NICKEL METALLOCENTER.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: RESIDUE IMPLICATED IN CATALYSIS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 574
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 575
DBREF 1FWA A 1 100 UNP P18316 URE3_KLEAE 1 100
DBREF 1FWA B 1 106 UNP P18315 URE2_KLEAE 1 106
DBREF 1FWA C 1 567 UNP P18314 URE1_KLEAE 1 567
SEQADV 1FWA KCX C 217 UNP P18314 LYS 217 MODIFIED RESIDUE
SEQADV 1FWA ALA C 319 UNP P18314 CYS 319 ENGINEERED MUTATION
SEQRES 1 A 100 MET GLU LEU THR PRO ARG GLU LYS ASP LYS LEU LEU LEU
SEQRES 2 A 100 PHE THR ALA ALA LEU VAL ALA GLU ARG ARG LEU ALA ARG
SEQRES 3 A 100 GLY LEU LYS LEU ASN TYR PRO GLU SER VAL ALA LEU ILE
SEQRES 4 A 100 SER ALA PHE ILE MET GLU GLY ALA ARG ASP GLY LYS SER
SEQRES 5 A 100 VAL ALA SER LEU MET GLU GLU GLY ARG HIS VAL LEU THR
SEQRES 6 A 100 ARG GLU GLN VAL MET GLU GLY VAL PRO GLU MET ILE PRO
SEQRES 7 A 100 ASP ILE GLN VAL GLU ALA THR PHE PRO ASP GLY SER LYS
SEQRES 8 A 100 LEU VAL THR VAL HIS ASN PRO ILE ILE
SEQRES 1 B 106 MET ILE PRO GLY GLU TYR HIS VAL LYS PRO GLY GLN ILE
SEQRES 2 B 106 ALA LEU ASN THR GLY ARG ALA THR CYS ARG VAL VAL VAL
SEQRES 3 B 106 GLU ASN HIS GLY ASP ARG PRO ILE GLN VAL GLY SER HIS
SEQRES 4 B 106 TYR HIS PHE ALA GLU VAL ASN PRO ALA LEU LYS PHE ASP
SEQRES 5 B 106 ARG GLN GLN ALA ALA GLY TYR ARG LEU ASN ILE PRO ALA
SEQRES 6 B 106 GLY THR ALA VAL ARG PHE GLU PRO GLY GLN LYS ARG GLU
SEQRES 7 B 106 VAL GLU LEU VAL ALA PHE ALA GLY HIS ARG ALA VAL PHE
SEQRES 8 B 106 GLY PHE ARG GLY GLU VAL MET GLY PRO LEU GLU VAL ASN
SEQRES 9 B 106 ASP GLU
SEQRES 1 C 567 MET SER ASN ILE SER ARG GLN ALA TYR ALA ASP MET PHE
SEQRES 2 C 567 GLY PRO THR VAL GLY ASP LYS VAL ARG LEU ALA ASP THR
SEQRES 3 C 567 GLU LEU TRP ILE GLU VAL GLU ASP ASP LEU THR THR TYR
SEQRES 4 C 567 GLY GLU GLU VAL LYS PHE GLY GLY GLY LYS VAL ILE ARG
SEQRES 5 C 567 ASP GLY MET GLY GLN GLY GLN MET LEU ALA ALA ASP CYS
SEQRES 6 C 567 VAL ASP LEU VAL LEU THR ASN ALA LEU ILE VAL ASP HIS
SEQRES 7 C 567 TRP GLY ILE VAL LYS ALA ASP ILE GLY VAL LYS ASP GLY
SEQRES 8 C 567 ARG ILE PHE ALA ILE GLY LYS ALA GLY ASN PRO ASP ILE
SEQRES 9 C 567 GLN PRO ASN VAL THR ILE PRO ILE GLY ALA ALA THR GLU
SEQRES 10 C 567 VAL ILE ALA ALA GLU GLY LYS ILE VAL THR ALA GLY GLY
SEQRES 11 C 567 ILE ASP THR HIS ILE HIS TRP ILE CYS PRO GLN GLN ALA
SEQRES 12 C 567 GLU GLU ALA LEU VAL SER GLY VAL THR THR MET VAL GLY
SEQRES 13 C 567 GLY GLY THR GLY PRO ALA ALA GLY THR HIS ALA THR THR
SEQRES 14 C 567 CYS THR PRO GLY PRO TRP TYR ILE SER ARG MET LEU GLN
SEQRES 15 C 567 ALA ALA ASP SER LEU PRO VAL ASN ILE GLY LEU LEU GLY
SEQRES 16 C 567 LYS GLY ASN VAL SER GLN PRO ASP ALA LEU ARG GLU GLN
SEQRES 17 C 567 VAL ALA ALA GLY VAL ILE GLY LEU KCX ILE HIS GLU ASP
SEQRES 18 C 567 TRP GLY ALA THR PRO ALA ALA ILE ASP CYS ALA LEU THR
SEQRES 19 C 567 VAL ALA ASP GLU MET ASP ILE GLN VAL ALA LEU HIS SER
SEQRES 20 C 567 ASP THR LEU ASN GLU SER GLY PHE VAL GLU ASP THR LEU
SEQRES 21 C 567 ALA ALA ILE GLY GLY ARG THR ILE HIS THR PHE HIS THR
SEQRES 22 C 567 GLU GLY ALA GLY GLY GLY HIS ALA PRO ASP ILE ILE THR
SEQRES 23 C 567 ALA CYS ALA HIS PRO ASN ILE LEU PRO SER SER THR ASN
SEQRES 24 C 567 PRO THR LEU PRO TYR THR LEU ASN THR ILE ASP GLU HIS
SEQRES 25 C 567 LEU ASP MET LEU MET VAL ALA HIS HIS LEU ASP PRO ASP
SEQRES 26 C 567 ILE ALA GLU ASP VAL ALA PHE ALA GLU SER ARG ILE ARG
SEQRES 27 C 567 ARG GLU THR ILE ALA ALA GLU ASP VAL LEU HIS ASP LEU
SEQRES 28 C 567 GLY ALA PHE SER LEU THR SER SER ASP SER GLN ALA MET
SEQRES 29 C 567 GLY ARG VAL GLY GLU VAL ILE LEU ARG THR TRP GLN VAL
SEQRES 30 C 567 ALA HIS ARG MET LYS VAL GLN ARG GLY ALA LEU ALA GLU
SEQRES 31 C 567 GLU THR GLY ASP ASN ASP ASN PHE ARG VAL LYS ARG TYR
SEQRES 32 C 567 ILE ALA LYS TYR THR ILE ASN PRO ALA LEU THR HIS GLY
SEQRES 33 C 567 ILE ALA HIS GLU VAL GLY SER ILE GLU VAL GLY LYS LEU
SEQRES 34 C 567 ALA ASP LEU VAL VAL TRP SER PRO ALA PHE PHE GLY VAL
SEQRES 35 C 567 LYS PRO ALA THR VAL ILE LYS GLY GLY MET ILE ALA ILE
SEQRES 36 C 567 ALA PRO MET GLY ASP ILE ASN ALA SER ILE PRO THR PRO
SEQRES 37 C 567 GLN PRO VAL HIS TYR ARG PRO MET PHE GLY ALA LEU GLY
SEQRES 38 C 567 SER ALA ARG HIS HIS CYS ARG LEU THR PHE LEU SER GLN
SEQRES 39 C 567 ALA ALA ALA ALA ASN GLY VAL ALA GLU ARG LEU ASN LEU
SEQRES 40 C 567 ARG SER ALA ILE ALA VAL VAL LYS GLY CYS ARG THR VAL
SEQRES 41 C 567 GLN LYS ALA ASP MET VAL HIS ASN SER LEU GLN PRO ASN
SEQRES 42 C 567 ILE THR VAL ASP ALA GLN THR TYR GLU VAL ARG VAL ASP
SEQRES 43 C 567 GLY GLU LEU ILE THR SER GLU PRO ALA ASP VAL LEU PRO
SEQRES 44 C 567 MET ALA GLN ARG TYR PHE LEU PHE
MODRES 1FWA KCX C 217 LYS LYSINE NZ-CARBOXYLIC ACID
HET KCX C 217 12
HET NI C 574 1
HET NI C 575 1
HET CO3 C 999 4
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM NI NICKEL (II) ION
HETNAM CO3 CARBONATE ION
FORMUL 3 KCX C7 H14 N2 O4
FORMUL 4 NI 2(NI 2+)
FORMUL 6 CO3 C O3 2-
FORMUL 7 HOH *281(H2 O)
HELIX 1 1 PRO A 5 ARG A 26 1 22
HELIX 2 2 TYR A 32 ASP A 49 1 18
HELIX 3 3 VAL A 53 HIS A 62 1 10
HELIX 4 4 ARG A 66 GLN A 68 5 3
HELIX 5 5 VAL A 73 MET A 76 1 4
HELIX 6 6 PHE B 42 GLU B 44 5 3
HELIX 7 7 ARG C 6 PHE C 13 1 8
HELIX 8 8 ALA C 62 ASP C 64 5 3
HELIX 9 9 PRO C 140 SER C 149 5 10
HELIX 10 10 ALA C 163 ALA C 167 1 5
HELIX 11 11 GLY C 173 SER C 186 1 14
HELIX 12 12 PRO C 202 ALA C 211 1 10
HELIX 13 13 GLU C 220 TRP C 222 5 3
HELIX 14 14 PRO C 226 MET C 239 1 14
HELIX 15 15 VAL C 256 ILE C 263 1 8
HELIX 16 16 ILE C 284 ALA C 289 5 6
HELIX 17 17 THR C 308 HIS C 320 1 13
HELIX 18 18 ALA C 327 ARG C 336 1 10
HELIX 19 19 ARG C 339 LEU C 351 1 13
HELIX 20 20 VAL C 370 ARG C 385 1 16
HELIX 21 21 ASN C 397 TYR C 407 1 11
HELIX 22 22 ILE C 409 THR C 414 1 6
HELIX 23 23 PRO C 437 PHE C 439 5 3
HELIX 24 24 PHE C 477 ALA C 479 5 3
HELIX 25 25 GLY C 481 CYS C 487 1 7
HELIX 26 26 GLN C 494 ALA C 498 1 5
HELIX 27 27 VAL C 501 LEU C 505 1 5
HELIX 28 28 LYS C 522 ASP C 524 5 3
SHEET 1 A 2 ASP A 79 PHE A 86 0
SHEET 2 A 2 GLY A 89 HIS A 96 -1 N VAL A 95 O ILE A 80
SHEET 1 B 3 THR B 21 GLU B 27 0
SHEET 2 B 3 LYS B 76 ALA B 83 -1 N LEU B 81 O CYS B 22
SHEET 3 B 3 TYR B 59 LEU B 61 -1 N ARG B 60 O VAL B 82
SHEET 1 C 2 ILE B 34 GLY B 37 0
SHEET 2 C 2 ALA B 68 PHE B 71 -1 N PHE B 71 O ILE B 34
SHEET 1 D 2 LYS C 20 ARG C 22 0
SHEET 2 D 2 TRP C 29 GLU C 31 -1 N ILE C 30 O VAL C 21
SHEET 1 E 4 GLU C 117 ALA C 120 0
SHEET 2 E 4 LEU C 68 THR C 71 1 N VAL C 69 O GLU C 117
SHEET 3 E 4 ASP C 85 LYS C 89 -1 N VAL C 88 O LEU C 68
SHEET 4 E 4 ARG C 92 GLY C 97 -1 N GLY C 97 O ASP C 85
SHEET 1 F 2 ALA C 73 ASP C 77 0
SHEET 2 F 2 GLY C 80 ALA C 84 -1 N ALA C 84 O ALA C 73
SHEET 1 G 5 LYS C 124 ALA C 128 0
SHEET 2 G 5 LEU C 432 SER C 436 -1 N TRP C 435 O ILE C 125
SHEET 3 G 5 THR C 446 LYS C 449 -1 N ILE C 448 O LEU C 432
SHEET 4 G 5 MET C 452 MET C 458 -1 N ILE C 455 O VAL C 447
SHEET 5 G 5 HIS C 472 PRO C 475 -1 N ARG C 474 O ALA C 456
SHEET 1 H 3 ASN C 190 LEU C 193 0
SHEET 2 H 3 VAL C 151 GLY C 156 1 N MET C 154 O ASN C 190
SHEET 3 H 3 GLY C 130 ASP C 132 1 N GLY C 130 O THR C 152
SHEET 1 I 3 LEU C 194 LYS C 196 0
SHEET 2 I 3 GLY C 215 HIS C 219 1 N GLY C 215 O GLY C 195
SHEET 3 I 3 GLN C 242 HIS C 246 1 N GLN C 242 O LEU C 216
SHEET 1 J 2 ILE C 268 THR C 270 0
SHEET 2 J 2 ILE C 293 PRO C 295 1 N LEU C 294 O ILE C 268
SHEET 1 K 2 LEU C 489 LEU C 492 0
SHEET 2 K 2 ALA C 510 VAL C 513 1 N ALA C 510 O THR C 490
SHEET 1 L 2 ILE C 534 VAL C 536 0
SHEET 2 L 2 VAL C 543 VAL C 545 -1 N ARG C 544 O THR C 535
LINK C LEU C 216 N KCX C 217 1555 1555 1.32
LINK C KCX C 217 N ILE C 218 1555 1555 1.33
LINK NE2 HIS C 134 NI NI C 575 1555 1555 2.29
LINK NE2 HIS C 136 NI NI C 575 1555 1555 2.14
LINK OQ1 KCX C 217 NI NI C 574 1555 1555 2.03
LINK OQ2 KCX C 217 NI NI C 575 1555 1555 2.09
LINK ND1 HIS C 246 NI NI C 574 1555 1555 2.24
LINK NE2 HIS C 272 NI NI C 574 1555 1555 2.30
LINK OD1 ASP C 360 NI NI C 575 1555 1555 2.17
LINK NI NI C 574 O1 CO3 C 999 1555 1555 2.15
LINK NI NI C 574 O2 CO3 C 999 1555 1555 2.33
LINK NI NI C 574 O HOH C1228 1555 1555 2.07
LINK NI NI C 574 O HOH C1229 1555 1555 2.18
LINK NI NI C 575 O1 CO3 C 999 1555 1555 2.01
LINK NI NI C 575 O3 CO3 C 999 1555 1555 2.33
LINK NI NI C 575 O HOH C1228 1555 1555 2.08
LINK NI NI C 575 O HOH C1230 1555 1555 2.15
CISPEP 1 ALA C 281 PRO C 282 0 0.10
CISPEP 2 LEU C 302 PRO C 303 0 -1.33
CISPEP 3 GLN C 469 PRO C 470 0 -0.09
SITE 1 NIL 11 NI C 574 NI C 575 HIS C 134 HIS C 136
SITE 2 NIL 11 KCX C 217 HIS C 246 HIS C 272 ASP C 360
SITE 3 NIL 11 HOH C1228 HOH C1229 HOH C1230
SITE 1 ACT 2 HIS C 219 HIS C 320
SITE 1 AC1 7 KCX C 217 HIS C 219 HIS C 246 HIS C 272
SITE 2 AC1 7 GLY C 277 HOH C1228 HOH C1229
SITE 1 AC2 6 HIS C 134 HIS C 136 KCX C 217 ASP C 360
SITE 2 AC2 6 HOH C1228 HOH C1230
CRYST1 170.800 170.800 170.800 90.00 90.00 90.00 I 21 3 24
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 0.005855 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005855 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005855 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
