HEADER HYDROLASE 04-MAR-00 1EJR
TITLE CRYSTAL STRUCTURE OF THE D221A VARIANT OF KLEBSIELLA AEROGENES UREASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UREASE ALPHA SUBUNIT;
COMPND 3 CHAIN: C;
COMPND 4 EC: 3.5.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: UREASE BETA SUBUNIT;
COMPND 9 CHAIN: B;
COMPND 10 EC: 3.5.1.5;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: UREASE GAMMA SUBUNIT;
COMPND 14 CHAIN: A;
COMPND 15 EC: 3.5.1.5;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA AEROGENES;
SOURCE 3 ORGANISM_TAXID: 28451;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: KLEBSIELLA AEROGENES;
SOURCE 8 ORGANISM_TAXID: 28451;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: KLEBSIELLA AEROGENES;
SOURCE 13 ORGANISM_TAXID: 28451;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-BETA BARREL, NICKEL METALLOENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.PEARSON,I.S.PARK,R.A.SCHALLER,L.O.MICHEL,P.A.KARPLUS,
AUTHOR 2 R.P.HAUSINGER
REVDAT 5 03-NOV-21 1EJR 1 REMARK SEQADV LINK
REVDAT 4 04-OCT-17 1EJR 1 REMARK
REVDAT 3 13-JUL-11 1EJR 1 VERSN
REVDAT 2 24-FEB-09 1EJR 1 VERSN
REVDAT 1 08-SEP-00 1EJR 0
JRNL AUTH M.A.PEARSON,I.S.PARK,R.A.SCHALLER,L.O.MICHEL,P.A.KARPLUS,
JRNL AUTH 2 R.P.HAUSINGER
JRNL TITL KINETIC AND STRUCTURAL CHARACTERIZATION OF UREASE ACTIVE
JRNL TITL 2 SITE VARIANTS.
JRNL REF BIOCHEMISTRY V. 39 8575 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10913264
JRNL DOI 10.1021/BI000613O
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.161
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 : 5686
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 405
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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: NULL
REMARK 4
REMARK 4 1EJR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010649.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 298; 298
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; N
REMARK 200 RADIATION SOURCE : ROTATING ANODE; ROTATING ANODE
REMARK 200 BEAMLINE : NULL; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 1.5418
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV; RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55503
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : NULL
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
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: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, HEPES, EDTA, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K. LITHIUM SULFATE,
REMARK 280 HEPES, EDTA, FORMATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 85.30000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 85.30000
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 85.30000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 85.30000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 85.30000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 85.30000
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 85.30000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 85.30000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 85.30000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 85.30000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 85.30000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 85.30000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 85.30000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 85.30000
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 85.30000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 85.30000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 85.30000
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 85.30000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 85.30000
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 85.30000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 85.30000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 85.30000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 85.30000
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 85.30000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 85.30000
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: 46320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -311.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, B, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 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 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 C 1001
REMARK 465 VAL C 1318
REMARK 465 CYS C 1319
REMARK 465 HIS C 1320
REMARK 465 HIS C 1321
REMARK 465 LEU C 1322
REMARK 465 ASP C 1323
REMARK 465 PRO C 1324
REMARK 465 ASP C 1325
REMARK 465 ILE C 1326
REMARK 465 ALA C 1327
REMARK 465 GLU C 1328
REMARK 465 ASP C 1329
REMARK 465 VAL C 1330
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 501 O HOH C 502 2.00
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 LEU C1316 CA - CB - CG ANGL. DEV. = -15.6 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 C1024 -135.62 52.88
REMARK 500 MET C1055 -110.70 -101.51
REMARK 500 PRO C1188 23.41 -77.75
REMARK 500 ASP C1248 91.34 -68.39
REMARK 500 HIS C1272 62.94 28.57
REMARK 500 HIS C1280 116.47 -39.82
REMARK 500 SER C1359 -63.17 -97.20
REMARK 500 ASP C1360 49.47 84.78
REMARK 500 ALA C1363 53.66 -145.24
REMARK 500 MET C1364 51.75 81.05
REMARK 500 THR C1408 -87.70 -123.01
REMARK 500 ASP C1460 118.63 -38.75
REMARK 500 ALA C1561 -110.57 -129.50
REMARK 500 ALA B2085 -148.53 -121.67
REMARK 500 PHE B2093 -125.35 58.30
REMARK 500 VAL B2097 -71.51 -104.04
REMARK 500 ASN A3097 62.14 38.11
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 NI C4774 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 500 O
REMARK 620 2 HOH C 501 O 64.2
REMARK 620 3 KCX C1217 OQ1 101.8 109.4
REMARK 620 4 HIS C1246 ND1 151.2 89.8 98.4
REMARK 620 5 HIS C1272 NE2 96.6 139.6 109.3 95.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C4775 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 500 O
REMARK 620 2 HOH C 502 O 58.5
REMARK 620 3 HIS C1134 NE2 97.8 154.8
REMARK 620 4 HIS C1136 NE2 147.5 89.1 113.9
REMARK 620 5 KCX C1217 OQ2 96.0 101.9 88.3 92.0
REMARK 620 6 ASP C1360 OD1 92.4 86.7 85.6 83.5 170.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 4774
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 4775
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EJS RELATED DB: PDB
REMARK 900 RELATED ID: 1EJT RELATED DB: PDB
REMARK 900 RELATED ID: 1EJU RELATED DB: PDB
REMARK 900 RELATED ID: 1EJV RELATED DB: PDB
REMARK 900 RELATED ID: 1EJW RELATED DB: PDB
REMARK 900 RELATED ID: 1EJX RELATED DB: PDB
DBREF 1EJR C 1001 1567 UNP P18314 URE1_KLEAE 1 567
DBREF 1EJR B 2001 2101 UNP P18315 URE2_KLEAE 1 101
DBREF 1EJR A 3001 3100 UNP P18316 URE3_KLEAE 1 100
SEQADV 1EJR KCX C 1217 UNP P18314 LYS 217 MODIFIED RESIDUE
SEQADV 1EJR ALA C 1221 UNP P18314 ASP 221 ENGINEERED MUTATION
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 ALA
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 CYS 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
SEQRES 1 B 101 MET ILE PRO GLY GLU TYR HIS VAL LYS PRO GLY GLN ILE
SEQRES 2 B 101 ALA LEU ASN THR GLY ARG ALA THR CYS ARG VAL VAL VAL
SEQRES 3 B 101 GLU ASN HIS GLY ASP ARG PRO ILE GLN VAL GLY SER HIS
SEQRES 4 B 101 TYR HIS PHE ALA GLU VAL ASN PRO ALA LEU LYS PHE ASP
SEQRES 5 B 101 ARG GLN GLN ALA ALA GLY TYR ARG LEU ASN ILE PRO ALA
SEQRES 6 B 101 GLY THR ALA VAL ARG PHE GLU PRO GLY GLN LYS ARG GLU
SEQRES 7 B 101 VAL GLU LEU VAL ALA PHE ALA GLY HIS ARG ALA VAL PHE
SEQRES 8 B 101 GLY PHE ARG GLY GLU VAL MET GLY PRO LEU
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
MODRES 1EJR KCX C 1217 LYS LYSINE NZ-CARBOXYLIC ACID
HET KCX C1217 12
HET NI C4774 1
HET NI C4775 1
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM NI NICKEL (II) ION
FORMUL 1 KCX C7 H14 N2 O4
FORMUL 4 NI 2(NI 2+)
FORMUL 6 HOH *405(H2 O)
HELIX 1 1 ARG C 1006 GLY C 1014 1 9
HELIX 2 2 LEU C 1061 CYS C 1065 5 5
HELIX 3 3 GLN C 1141 GLY C 1150 1 10
HELIX 4 4 ALA C 1162 THR C 1168 1 7
HELIX 5 5 PRO C 1172 ASP C 1185 1 14
HELIX 6 6 GLN C 1201 GLY C 1212 1 12
HELIX 7 7 ALA C 1221 GLY C 1223 5 3
HELIX 8 8 THR C 1225 ASP C 1240 1 16
HELIX 9 9 PHE C 1255 GLY C 1264 1 10
HELIX 10 10 ASP C 1283 HIS C 1290 5 8
HELIX 11 11 PRO C 1300 LEU C 1302 5 3
HELIX 12 12 ASN C 1307 MET C 1317 1 11
HELIX 13 13 PHE C 1332 ILE C 1337 1 6
HELIX 14 14 ARG C 1338 LEU C 1351 1 14
HELIX 15 15 GLU C 1369 GLY C 1386 1 18
HELIX 16 16 ASP C 1396 LYS C 1406 1 11
HELIX 17 17 THR C 1408 HIS C 1415 1 8
HELIX 18 18 SER C 1436 PHE C 1440 5 5
HELIX 19 19 PHE C 1477 ALA C 1479 5 3
HELIX 20 20 LEU C 1480 ARG C 1488 1 9
HELIX 21 21 SER C 1493 ASN C 1499 1 7
HELIX 22 22 GLY C 1500 ASN C 1506 1 7
HELIX 23 23 GLN C 1521 MET C 1525 5 5
HELIX 24 24 HIS B 2041 VAL B 2045 5 5
HELIX 25 25 THR A 3004 ARG A 3026 1 23
HELIX 26 26 ASN A 3031 GLY A 3050 1 20
HELIX 27 27 SER A 3052 GLY A 3060 1 9
HELIX 28 28 ARG A 3061 VAL A 3063 5 3
HELIX 29 29 THR A 3065 GLN A 3068 5 4
HELIX 30 30 GLY A 3072 ILE A 3077 1 6
SHEET 1 A 2 ASN C1003 SER C1005 0
SHEET 2 A 2 GLN B2012 ALA B2014 -1 N ILE B2013 O ILE C1004
SHEET 1 B 3 TRP C1029 GLU C1031 0
SHEET 2 B 3 LYS C1020 ARG C1022 -1 O VAL C1021 N ILE C1030
SHEET 3 B 3 TYR B2006 HIS B2007 -1 N HIS B2007 O LYS C1020
SHEET 1 C12 ASP C1034 ASP C1035 0
SHEET 2 C12 GLY C1080 LYS C1089 1 O ILE C1081 N ASP C1034
SHEET 3 C12 ARG C1092 GLY C1097 -1 O ARG C1092 N LYS C1089
SHEET 4 C12 GLY C1080 LYS C1089 -1 N ASP C1085 O GLY C1097
SHEET 5 C12 LEU C1068 ASP C1077 -1 O LEU C1068 N VAL C1088
SHEET 6 C12 GLU C1117 ALA C1120 1 O GLU C1117 N VAL C1069
SHEET 7 C12 LEU C1068 ASP C1077 1 O VAL C1069 N ILE C1119
SHEET 8 C12 ILE C1125 ALA C1128 1 N VAL C1126 O LEU C1074
SHEET 9 C12 LEU C1432 TRP C1435 -1 N VAL C1433 O THR C1127
SHEET 10 C12 THR C1446 LYS C1449 -1 O THR C1446 N VAL C1434
SHEET 11 C12 MET C1452 MET C1458 -1 O MET C1452 N LYS C1449
SHEET 12 C12 HIS C1472 PRO C1475 -1 O HIS C1472 N MET C1458
SHEET 1 D 2 ALA C1099 GLY C1100 0
SHEET 2 D 2 ILE C1110 PRO C1111 1 O ILE C1110 N GLY C1100
SHEET 1 E 3 GLY C1130 HIS C1136 0
SHEET 2 E 3 VAL C1151 GLY C1157 1 N THR C1152 O GLY C1130
SHEET 3 E 3 ASN C1190 LEU C1193 1 O ASN C1190 N MET C1154
SHEET 1 F 5 GLY C1215 HIS C1219 0
SHEET 2 F 5 GLN C1242 HIS C1246 1 O GLN C1242 N LEU C1216
SHEET 3 F 5 ILE C1268 THR C1270 1 N HIS C1269 O VAL C1243
SHEET 4 F 5 ILE C1293 THR C1298 1 N LEU C1294 O ILE C1268
SHEET 5 F 5 LEU C1356 SER C1358 1 O LEU C1356 N SER C1297
SHEET 1 G 2 LEU C1489 LEU C1492 0
SHEET 2 G 2 ALA C1510 VAL C1513 1 O ALA C1510 N THR C1490
SHEET 1 H 3 ILE C1534 VAL C1536 0
SHEET 2 H 3 VAL C1543 VAL C1545 -1 O ARG C1544 N THR C1535
SHEET 3 H 3 GLU C1548 LEU C1549 -1 O GLU C1548 N VAL C1545
SHEET 1 I 4 LEU B2049 LYS B2050 0
SHEET 2 I 4 THR B2021 ASN B2028 -1 O GLU B2027 N LYS B2050
SHEET 3 I 4 LYS B2076 ALA B2083 -1 O ARG B2077 N VAL B2026
SHEET 4 I 4 TYR B2059 LEU B2061 -1 O ARG B2060 N VAL B2082
SHEET 1 J 2 ILE B2034 GLY B2037 0
SHEET 2 J 2 ALA B2068 PHE B2071 -1 O VAL B2069 N VAL B2036
SHEET 1 K 2 ALA B2089 VAL B2090 0
SHEET 2 K 2 GLY B2099 PRO B2100 -1 O GLY B2099 N VAL B2090
SHEET 1 L 2 ASP A3079 PHE A3086 0
SHEET 2 L 2 GLY A3089 HIS A3096 -1 O GLY A3089 N PHE A3086
LINK C LEU C1216 N KCX C1217 1555 1555 1.32
LINK C KCX C1217 N ILE C1218 1555 1555 1.33
LINK O HOH C 500 NI NI C4774 1555 1555 2.06
LINK O HOH C 500 NI NI C4775 1555 1555 2.10
LINK O HOH C 501 NI NI C4774 1555 1555 2.54
LINK O HOH C 502 NI NI C4775 1555 1555 2.41
LINK NE2 HIS C1134 NI NI C4775 1555 1555 2.21
LINK NE2 HIS C1136 NI NI C4775 1555 1555 2.11
LINK OQ1 KCX C1217 NI NI C4774 1555 1555 2.04
LINK OQ2 KCX C1217 NI NI C4775 1555 1555 2.19
LINK ND1 HIS C1246 NI NI C4774 1555 1555 2.09
LINK NE2 HIS C1272 NI NI C4774 1555 1555 2.25
LINK OD1 ASP C1360 NI NI C4775 1555 1555 2.12
CISPEP 1 ALA C 1281 PRO C 1282 0 -2.06
CISPEP 2 LEU C 1302 PRO C 1303 0 0.10
CISPEP 3 GLN C 1469 PRO C 1470 0 -0.18
SITE 1 AC1 8 HOH C 500 HOH C 501 KCX C1217 HIS C1219
SITE 2 AC1 8 HIS C1246 HIS C1272 GLY C1277 NI C4775
SITE 1 AC2 7 HOH C 500 HOH C 502 HIS C1134 HIS C1136
SITE 2 AC2 7 KCX C1217 ASP C1360 NI C4774
CRYST1 170.600 170.600 170.600 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 0.005862 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005862 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005862 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
