HEADER ISOMERASE 15-OCT-04 1XRU
TITLE CRYSTAL STRUCTURE OF 5-KETO-4-DEOXYURONATE ISOMERASE FROM ESCHERICIA
TITLE 2 COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-DEOXY-L-THREO-5-HEXOSULOSE-URONATE KETOL-ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 5-KETO-4-DEOXYURONATE ISOMERASE, DKI ISOMERASE;
COMPND 5 EC: 5.3.1.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: KDUI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BETA BARREL, CUPIN, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.L.CROWTHER,M.M.GEORGIADIS
REVDAT 5 13-JUL-11 1XRU 1 VERSN
REVDAT 4 24-FEB-09 1XRU 1 VERSN
REVDAT 3 01-NOV-05 1XRU 1 JRNL
REVDAT 2 27-SEP-05 1XRU 1 JRNL
REVDAT 1 05-APR-05 1XRU 0
JRNL AUTH R.L.CROWTHER,M.M.GEORGIADIS
JRNL TITL THE CRYSTAL STRUCTURE OF 5-KETO-4-DEOXYURONATE ISOMERASE
JRNL TITL 2 FROM ESCHERICHIA COLI
JRNL REF PROTEINS V. 61 680 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 16152643
JRNL DOI 10.1002/PROT.20598
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.97
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) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 51449
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2562
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 : 4374
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 457
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -0.40000
REMARK 3 B12 (A**2) : 0.61000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
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) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1XRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030693.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980122, 0.979634, 0.979538
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51573
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.20000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, CALCIUM CHLORIDE, HEPES, PH
REMARK 280 7, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.48600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.72546
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.95400
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 51.48600
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 29.72546
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 58.95400
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 51.48600
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 29.72546
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 58.95400
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.45091
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 117.90800
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 59.45091
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 117.90800
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 59.45091
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 117.90800
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXAMER GENERATED FROM THE
REMARK 300 DIMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: -Y, X-Y, Z AND Y-X,
REMARK 300 -X, Z.
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 102.97200
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 350 BIOMT1 3 -0.500000 0.866025 0.000000 51.48600
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 89.17637
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 102.97200
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 ALA A 279
REMARK 465 ALA B 279
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 62 CG CD OE1 OE2
REMARK 470 ALA A 273 CB
REMARK 470 ASP B 119 CG OD1 OD2
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 ILE A 53 -70.60 -126.06
REMARK 500 GLU A 146 -9.63 -57.25
REMARK 500 SER A 148 79.88 55.82
REMARK 500 GLN A 176 -10.43 -151.34
REMARK 500 GLU A 225 54.61 -140.62
REMARK 500 ILE B 53 -64.65 -122.12
REMARK 500 GLN B 176 -9.57 -148.32
REMARK 500 GLU B 225 52.01 -141.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 668 DISTANCE = 5.49 ANGSTROMS
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 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 245 NE2
REMARK 620 2 GLU A 203 OE1 104.6
REMARK 620 3 HIS A 198 NE2 106.9 115.7
REMARK 620 4 HIS A 196 NE2 105.2 113.8 109.7
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 HIS B 198 NE2
REMARK 620 2 HIS B 245 NE2 105.6
REMARK 620 3 HIS B 196 NE2 112.3 105.6
REMARK 620 4 GLU B 203 OE2 116.1 102.8 113.1
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 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 504
REMARK 999
REMARK 999 SEQUENCE AUTHOR STATES THAT THE C-TERMINAL DIFFERENCES FROM
REMARK 999 DATABASE SEQUENCE IS A NEUTRAL DESIGNATION. THE C-TERMINAL SEQUENCE
REMARK 999 REPORTED HERE IS INDEED CORRECT FOR THE GENE THAT WAS CLONED AND
REMARK 999 FOR PROTEIN THAT WAS CRYSTALLIZED.
DBREF 1XRU A 1 278 UNP Q46938 KDUI_ECOLI 1 278
DBREF 1XRU B 1 278 UNP Q46938 KDUI_ECOLI 1 278
SEQADV 1XRU GLY A -2 UNP Q46938 CLONING ARTIFACT
SEQADV 1XRU SER A -1 UNP Q46938 CLONING ARTIFACT
SEQADV 1XRU ALA A 0 UNP Q46938 CLONING ARTIFACT
SEQADV 1XRU MSE A 37 UNP Q46938 MET 37 MODIFIED RESIDUE
SEQADV 1XRU MSE A 51 UNP Q46938 MET 51 MODIFIED RESIDUE
SEQADV 1XRU MSE A 179 UNP Q46938 MET 179 MODIFIED RESIDUE
SEQADV 1XRU MSE A 193 UNP Q46938 MET 193 MODIFIED RESIDUE
SEQADV 1XRU MSE A 202 UNP Q46938 MET 202 MODIFIED RESIDUE
SEQADV 1XRU MSE A 210 UNP Q46938 MET 210 MODIFIED RESIDUE
SEQADV 1XRU MSE A 219 UNP Q46938 MET 219 MODIFIED RESIDUE
SEQADV 1XRU MSE A 220 UNP Q46938 MET 220 MODIFIED RESIDUE
SEQADV 1XRU MSE A 231 UNP Q46938 MET 231 MODIFIED RESIDUE
SEQADV 1XRU MSE A 259 UNP Q46938 MET 259 MODIFIED RESIDUE
SEQADV 1XRU MSE A 269 UNP Q46938 MET 269 MODIFIED RESIDUE
SEQADV 1XRU GLU A 276 UNP Q46938 ASP 276 SEE REMARK 999
SEQADV 1XRU ILE A 277 UNP Q46938 LEU 277 SEE REMARK 999
SEQADV 1XRU CYS A 278 UNP Q46938 ARG 278 SEE REMARK 999
SEQADV 1XRU ALA A 279 UNP Q46938 SEE REMARK 999
SEQADV 1XRU GLY B -2 UNP Q46938 CLONING ARTIFACT
SEQADV 1XRU SER B -1 UNP Q46938 CLONING ARTIFACT
SEQADV 1XRU ALA B 0 UNP Q46938 CLONING ARTIFACT
SEQADV 1XRU MSE B 37 UNP Q46938 MET 37 MODIFIED RESIDUE
SEQADV 1XRU MSE B 51 UNP Q46938 MET 51 MODIFIED RESIDUE
SEQADV 1XRU MSE B 179 UNP Q46938 MET 179 MODIFIED RESIDUE
SEQADV 1XRU MSE B 193 UNP Q46938 MET 193 MODIFIED RESIDUE
SEQADV 1XRU MSE B 202 UNP Q46938 MET 202 MODIFIED RESIDUE
SEQADV 1XRU MSE B 210 UNP Q46938 MET 210 MODIFIED RESIDUE
SEQADV 1XRU MSE B 219 UNP Q46938 MET 219 MODIFIED RESIDUE
SEQADV 1XRU MSE B 220 UNP Q46938 MET 220 MODIFIED RESIDUE
SEQADV 1XRU MSE B 231 UNP Q46938 MET 231 MODIFIED RESIDUE
SEQADV 1XRU MSE B 259 UNP Q46938 MET 259 MODIFIED RESIDUE
SEQADV 1XRU MSE B 269 UNP Q46938 MET 269 MODIFIED RESIDUE
SEQADV 1XRU GLU B 276 UNP Q46938 ASP 276 SEE REMARK 999
SEQADV 1XRU ILE B 277 UNP Q46938 LEU 277 SEE REMARK 999
SEQADV 1XRU CYS B 278 UNP Q46938 ARG 278 SEE REMARK 999
SEQADV 1XRU ALA B 279 UNP Q46938 SEE REMARK 999
SEQRES 1 A 282 GLY SER ALA MET ASP VAL ARG GLN SER ILE HIS SER ALA
SEQRES 2 A 282 HIS ALA LYS THR LEU ASP THR GLN GLY LEU ARG ASN GLU
SEQRES 3 A 282 PHE LEU VAL GLU LYS VAL PHE VAL ALA ASP GLU TYR THR
SEQRES 4 A 282 MSE VAL TYR SER HIS ILE ASP ARG ILE ILE VAL GLY GLY
SEQRES 5 A 282 ILE MSE PRO ILE THR LYS THR VAL SER VAL GLY GLY GLU
SEQRES 6 A 282 VAL GLY LYS GLN LEU GLY VAL SER TYR PHE LEU GLU ARG
SEQRES 7 A 282 ARG GLU LEU GLY VAL ILE ASN ILE GLY GLY ALA GLY THR
SEQRES 8 A 282 ILE THR VAL ASP GLY GLN CYS TYR GLU ILE GLY HIS ARG
SEQRES 9 A 282 ASP ALA LEU TYR VAL GLY LYS GLY ALA LYS GLU VAL VAL
SEQRES 10 A 282 PHE ALA SER ILE ASP THR GLY THR PRO ALA LYS PHE TYR
SEQRES 11 A 282 TYR ASN CYS ALA PRO ALA HIS THR THR TYR PRO THR LYS
SEQRES 12 A 282 LYS VAL THR PRO ASP GLU VAL SER PRO VAL THR LEU GLY
SEQRES 13 A 282 ASP ASN LEU THR SER ASN ARG ARG THR ILE ASN LYS TYR
SEQRES 14 A 282 PHE VAL PRO ASP VAL LEU GLU THR CYS GLN LEU SER MSE
SEQRES 15 A 282 GLY LEU THR GLU LEU ALA PRO GLY ASN LEU TRP ASN THR
SEQRES 16 A 282 MSE PRO CYS HIS THR HIS GLU ARG ARG MSE GLU VAL TYR
SEQRES 17 A 282 PHE TYR PHE ASN MSE ASP ASP ASP ALA CYS VAL PHE HIS
SEQRES 18 A 282 MSE MSE GLY GLN PRO GLN GLU THR ARG HIS ILE VAL MSE
SEQRES 19 A 282 HIS ASN GLU GLN ALA VAL ILE SER PRO SER TRP SER ILE
SEQRES 20 A 282 HIS SER GLY VAL GLY THR LYS ALA TYR THR PHE ILE TRP
SEQRES 21 A 282 GLY MSE VAL GLY GLU ASN GLN VAL PHE ASP ASP MSE ASP
SEQRES 22 A 282 HIS VAL ALA VAL LYS GLU ILE CYS ALA
SEQRES 1 B 282 GLY SER ALA MET ASP VAL ARG GLN SER ILE HIS SER ALA
SEQRES 2 B 282 HIS ALA LYS THR LEU ASP THR GLN GLY LEU ARG ASN GLU
SEQRES 3 B 282 PHE LEU VAL GLU LYS VAL PHE VAL ALA ASP GLU TYR THR
SEQRES 4 B 282 MSE VAL TYR SER HIS ILE ASP ARG ILE ILE VAL GLY GLY
SEQRES 5 B 282 ILE MSE PRO ILE THR LYS THR VAL SER VAL GLY GLY GLU
SEQRES 6 B 282 VAL GLY LYS GLN LEU GLY VAL SER TYR PHE LEU GLU ARG
SEQRES 7 B 282 ARG GLU LEU GLY VAL ILE ASN ILE GLY GLY ALA GLY THR
SEQRES 8 B 282 ILE THR VAL ASP GLY GLN CYS TYR GLU ILE GLY HIS ARG
SEQRES 9 B 282 ASP ALA LEU TYR VAL GLY LYS GLY ALA LYS GLU VAL VAL
SEQRES 10 B 282 PHE ALA SER ILE ASP THR GLY THR PRO ALA LYS PHE TYR
SEQRES 11 B 282 TYR ASN CYS ALA PRO ALA HIS THR THR TYR PRO THR LYS
SEQRES 12 B 282 LYS VAL THR PRO ASP GLU VAL SER PRO VAL THR LEU GLY
SEQRES 13 B 282 ASP ASN LEU THR SER ASN ARG ARG THR ILE ASN LYS TYR
SEQRES 14 B 282 PHE VAL PRO ASP VAL LEU GLU THR CYS GLN LEU SER MSE
SEQRES 15 B 282 GLY LEU THR GLU LEU ALA PRO GLY ASN LEU TRP ASN THR
SEQRES 16 B 282 MSE PRO CYS HIS THR HIS GLU ARG ARG MSE GLU VAL TYR
SEQRES 17 B 282 PHE TYR PHE ASN MSE ASP ASP ASP ALA CYS VAL PHE HIS
SEQRES 18 B 282 MSE MSE GLY GLN PRO GLN GLU THR ARG HIS ILE VAL MSE
SEQRES 19 B 282 HIS ASN GLU GLN ALA VAL ILE SER PRO SER TRP SER ILE
SEQRES 20 B 282 HIS SER GLY VAL GLY THR LYS ALA TYR THR PHE ILE TRP
SEQRES 21 B 282 GLY MSE VAL GLY GLU ASN GLN VAL PHE ASP ASP MSE ASP
SEQRES 22 B 282 HIS VAL ALA VAL LYS GLU ILE CYS ALA
MODRES 1XRU MSE A 37 MET SELENOMETHIONINE
MODRES 1XRU MSE A 51 MET SELENOMETHIONINE
MODRES 1XRU MSE A 179 MET SELENOMETHIONINE
MODRES 1XRU MSE A 193 MET SELENOMETHIONINE
MODRES 1XRU MSE A 202 MET SELENOMETHIONINE
MODRES 1XRU MSE A 210 MET SELENOMETHIONINE
MODRES 1XRU MSE A 219 MET SELENOMETHIONINE
MODRES 1XRU MSE A 220 MET SELENOMETHIONINE
MODRES 1XRU MSE A 231 MET SELENOMETHIONINE
MODRES 1XRU MSE A 259 MET SELENOMETHIONINE
MODRES 1XRU MSE A 269 MET SELENOMETHIONINE
MODRES 1XRU MSE B 37 MET SELENOMETHIONINE
MODRES 1XRU MSE B 51 MET SELENOMETHIONINE
MODRES 1XRU MSE B 179 MET SELENOMETHIONINE
MODRES 1XRU MSE B 193 MET SELENOMETHIONINE
MODRES 1XRU MSE B 202 MET SELENOMETHIONINE
MODRES 1XRU MSE B 210 MET SELENOMETHIONINE
MODRES 1XRU MSE B 219 MET SELENOMETHIONINE
MODRES 1XRU MSE B 220 MET SELENOMETHIONINE
MODRES 1XRU MSE B 231 MET SELENOMETHIONINE
MODRES 1XRU MSE B 259 MET SELENOMETHIONINE
MODRES 1XRU MSE B 269 MET SELENOMETHIONINE
HET MSE A 37 8
HET MSE A 51 8
HET MSE A 179 8
HET MSE A 193 8
HET MSE A 202 8
HET MSE A 210 8
HET MSE A 219 8
HET MSE A 220 8
HET MSE A 231 8
HET MSE A 259 8
HET MSE A 269 8
HET MSE B 37 8
HET MSE B 51 8
HET MSE B 179 8
HET MSE B 193 8
HET MSE B 202 8
HET MSE B 210 8
HET MSE B 219 8
HET MSE B 220 8
HET MSE B 231 8
HET MSE B 259 8
HET MSE B 269 8
HET ZN A 501 1
HET ZN B 502 1
HET 1PE A 503 16
HET 1PE B 504 16
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 1PE 2(C10 H22 O6)
FORMUL 7 HOH *457(H2 O)
HELIX 1 1 HIS A 8 LYS A 13 1 6
HELIX 2 2 ASP A 16 PHE A 24 1 9
HELIX 3 3 GLY A 60 LEU A 67 1 8
HELIX 4 4 THR A 143 SER A 148 1 6
HELIX 5 5 ASP A 154 SER A 158 5 5
HELIX 6 6 ALA A 273 CYS A 278 1 6
HELIX 7 7 HIS B 8 LYS B 13 1 6
HELIX 8 8 ASP B 16 PHE B 24 1 9
HELIX 9 9 GLY B 60 LEU B 67 1 8
HELIX 10 10 THR B 143 VAL B 147 5 5
HELIX 11 11 ASP B 154 SER B 158 5 5
HELIX 12 12 ALA B 273 CYS B 278 1 6
SHEET 1 A 7 ASP A 2 ARG A 4 0
SHEET 2 A 7 VAL A 38 SER A 40 1 O TYR A 39 N ARG A 4
SHEET 3 A 7 ILE A 45 ILE A 50 -1 O VAL A 47 N VAL A 38
SHEET 4 A 7 PHE A 126 PRO A 132 -1 O CYS A 130 N ILE A 46
SHEET 5 A 7 ARG A 76 ASN A 82 -1 N GLU A 77 O ALA A 131
SHEET 6 A 7 ALA A 103 VAL A 106 -1 O VAL A 106 N LEU A 78
SHEET 7 A 7 LYS A 140 VAL A 142 -1 O LYS A 140 N TYR A 105
SHEET 1 B 7 LEU A 25 VAL A 26 0
SHEET 2 B 7 GLN A 235 SER A 239 -1 O ALA A 236 N VAL A 26
SHEET 3 B 7 ARG A 201 PHE A 208 -1 N TYR A 205 O VAL A 237
SHEET 4 B 7 THR A 254 GLY A 261 -1 O THR A 254 N PHE A 208
SHEET 5 B 7 SER A 178 LEU A 184 -1 N SER A 178 O MSE A 259
SHEET 6 B 7 ARG A 161 PHE A 167 -1 N ASN A 164 O LEU A 181
SHEET 7 B 7 VAL A 150 LEU A 152 -1 N VAL A 150 O ILE A 163
SHEET 1 C 4 VAL A 57 VAL A 59 0
SHEET 2 C 4 VAL A 113 SER A 117 -1 O PHE A 115 N VAL A 57
SHEET 3 C 4 GLY A 87 VAL A 91 -1 N THR A 90 O VAL A 114
SHEET 4 C 4 GLN A 94 ILE A 98 -1 O GLN A 94 N VAL A 91
SHEET 1 D 4 TRP A 190 ASN A 191 0
SHEET 2 D 4 ILE A 244 GLY A 249 -1 O GLY A 247 N ASN A 191
SHEET 3 D 4 VAL A 216 GLN A 222 -1 N MSE A 219 O SER A 246
SHEET 4 D 4 GLU A 225 MSE A 231 -1 O MSE A 231 N VAL A 216
SHEET 1 E 2 CYS A 195 THR A 197 0
SHEET 2 E 2 ASP A 270 VAL A 272 -1 O ASP A 270 N THR A 197
SHEET 1 F 7 ASP B 2 ARG B 4 0
SHEET 2 F 7 VAL B 38 SER B 40 1 O TYR B 39 N ARG B 4
SHEET 3 F 7 ILE B 45 ILE B 50 -1 O VAL B 47 N VAL B 38
SHEET 4 F 7 PHE B 126 PRO B 132 -1 O CYS B 130 N ILE B 46
SHEET 5 F 7 ARG B 76 ASN B 82 -1 N GLU B 77 O ALA B 131
SHEET 6 F 7 ALA B 103 VAL B 106 -1 O VAL B 106 N LEU B 78
SHEET 7 F 7 LYS B 140 VAL B 142 -1 O VAL B 142 N ALA B 103
SHEET 1 G 7 LEU B 25 VAL B 26 0
SHEET 2 G 7 GLN B 235 SER B 239 -1 O ALA B 236 N VAL B 26
SHEET 3 G 7 ARG B 201 PHE B 208 -1 N TYR B 205 O VAL B 237
SHEET 4 G 7 THR B 254 GLY B 261 -1 O THR B 254 N PHE B 208
SHEET 5 G 7 SER B 178 LEU B 184 -1 N THR B 182 O PHE B 255
SHEET 6 G 7 ARG B 161 PHE B 167 -1 N ASN B 164 O LEU B 181
SHEET 7 G 7 VAL B 150 LEU B 152 -1 N VAL B 150 O ILE B 163
SHEET 1 H 4 VAL B 57 VAL B 59 0
SHEET 2 H 4 VAL B 113 SER B 117 -1 O PHE B 115 N VAL B 57
SHEET 3 H 4 GLY B 87 VAL B 91 -1 N THR B 90 O VAL B 114
SHEET 4 H 4 GLN B 94 ILE B 98 -1 O GLN B 94 N VAL B 91
SHEET 1 I 2 CYS B 195 THR B 197 0
SHEET 2 I 2 ASP B 270 VAL B 272 -1 O ASP B 270 N THR B 197
SHEET 1 J 3 GLU B 225 MSE B 231 0
SHEET 2 J 3 VAL B 216 GLN B 222 -1 N MSE B 220 O ARG B 227
SHEET 3 J 3 ILE B 244 GLY B 249 -1 O SER B 246 N MSE B 219
LINK C THR A 36 N MSE A 37 1555 1555 1.32
LINK C MSE A 37 N VAL A 38 1555 1555 1.33
LINK C ILE A 50 N MSE A 51 1555 1555 1.33
LINK C MSE A 51 N PRO A 52 1555 1555 1.34
LINK C SER A 178 N MSE A 179 1555 1555 1.33
LINK C MSE A 179 N GLY A 180 1555 1555 1.33
LINK C THR A 192 N MSE A 193 1555 1555 1.33
LINK C MSE A 193 N PRO A 194 1555 1555 1.34
LINK C ARG A 201 N MSE A 202 1555 1555 1.33
LINK C MSE A 202 N GLU A 203 1555 1555 1.33
LINK C ASN A 209 N MSE A 210 1555 1555 1.33
LINK C MSE A 210 N ASP A 211 1555 1555 1.33
LINK C HIS A 218 N MSE A 219 1555 1555 1.33
LINK C MSE A 219 N MSE A 220 1555 1555 1.33
LINK C MSE A 220 N GLY A 221 1555 1555 1.33
LINK C VAL A 230 N MSE A 231 1555 1555 1.33
LINK C MSE A 231 N HIS A 232 1555 1555 1.33
LINK C GLY A 258 N MSE A 259 1555 1555 1.33
LINK C MSE A 259 N VAL A 260 1555 1555 1.33
LINK C ASP A 268 N MSE A 269 1555 1555 1.33
LINK C MSE A 269 N ASP A 270 1555 1555 1.33
LINK ZN ZN A 501 NE2 HIS A 245 1555 1555 2.04
LINK ZN ZN A 501 OE1 GLU A 203 1555 1555 1.88
LINK ZN ZN A 501 NE2 HIS A 198 1555 1555 2.08
LINK ZN ZN A 501 NE2 HIS A 196 1555 1555 2.23
LINK C THR B 36 N MSE B 37 1555 1555 1.32
LINK C MSE B 37 N VAL B 38 1555 1555 1.33
LINK C ILE B 50 N MSE B 51 1555 1555 1.33
LINK C MSE B 51 N PRO B 52 1555 1555 1.34
LINK C SER B 178 N MSE B 179 1555 1555 1.33
LINK C MSE B 179 N GLY B 180 1555 1555 1.33
LINK C THR B 192 N MSE B 193 1555 1555 1.33
LINK C MSE B 193 N PRO B 194 1555 1555 1.35
LINK C ARG B 201 N MSE B 202 1555 1555 1.33
LINK C MSE B 202 N GLU B 203 1555 1555 1.33
LINK C ASN B 209 N MSE B 210 1555 1555 1.33
LINK C MSE B 210 N ASP B 211 1555 1555 1.33
LINK C HIS B 218 N MSE B 219 1555 1555 1.33
LINK C MSE B 219 N MSE B 220 1555 1555 1.33
LINK C MSE B 220 N GLY B 221 1555 1555 1.33
LINK C VAL B 230 N MSE B 231 1555 1555 1.32
LINK C MSE B 231 N HIS B 232 1555 1555 1.33
LINK C GLY B 258 N MSE B 259 1555 1555 1.33
LINK C MSE B 259 N VAL B 260 1555 1555 1.33
LINK C ASP B 268 N MSE B 269 1555 1555 1.33
LINK C MSE B 269 N ASP B 270 1555 1555 1.33
LINK ZN ZN B 502 NE2 HIS B 198 1555 1555 2.07
LINK ZN ZN B 502 NE2 HIS B 245 1555 1555 2.08
LINK ZN ZN B 502 NE2 HIS B 196 1555 1555 2.22
LINK ZN ZN B 502 OE2 GLU B 203 1555 1555 1.91
CISPEP 1 MSE A 193 PRO A 194 0 0.01
CISPEP 2 MSE B 193 PRO B 194 0 0.03
SITE 1 AC1 4 HIS A 196 HIS A 198 GLU A 203 HIS A 245
SITE 1 AC2 4 HIS B 196 HIS B 198 GLU B 203 HIS B 245
SITE 1 AC3 6 ILE A 163 LYS A 165 VAL A 168 TRP A 257
SITE 2 AC3 6 PHE A 266 HOH A 712
SITE 1 AC4 7 ILE B 163 LYS B 165 VAL B 168 TRP B 257
SITE 2 AC4 7 PHE B 266 HOH B 682 HOH B 738
CRYST1 102.972 102.972 176.862 90.00 90.00 120.00 H 3 18
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 0.009711 0.005607 0.000000 0.00000
SCALE2 0.000000 0.011214 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005654 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
