HEADER LYASE 08-MAY-07 2PU0
TITLE CRYSTAL STRUCTURE OF THE T. BRUCEI ENOLASE COMPLEXED WITH
TITLE 2 PHOSPHONOACETOHYDROXAMATE (PAH), HIS156-IN CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 2-PHOSPHO-D-GLYCERATE HYDRO-LYASE;
COMPND 5 EC: 4.2.1.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5691;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS LYASE, GLYCOLYSIS, HIS-TAG
EXPDTA X-RAY DIFFRACTION
AUTHOR M.V.A.S.NAVARRO,D.J.RIGDEN,R.C.GARRATT,S.M.G.DIAS
REVDAT 4 30-AUG-23 2PU0 1 REMARK
REVDAT 3 20-OCT-21 2PU0 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2PU0 1 VERSN
REVDAT 1 20-NOV-07 2PU0 0
JRNL AUTH M.V.NAVARRO,S.M.GOMES DIAS,L.V.MELLO,M.T.DA SILVA GIOTTO,
JRNL AUTH 2 S.GAVALDA,C.BLONSKI,R.C.GARRATT,D.J.RIGDEN
JRNL TITL STRUCTURAL FLEXIBILITY IN TRYPANOSOMA BRUCEI ENOLASE
JRNL TITL 2 REVEALED BY X-RAY CRYSTALLOGRAPHY AND MOLECULAR DYNAMICS.
JRNL REF FEBS J. V. 274 5077 2007
JRNL REFN ISSN 1742-464X
JRNL PMID 17822439
JRNL DOI 10.1111/J.1742-4658.2007.06027.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.T.DA SILVA GIOTTO,V.HANNAERT,D.VERTOMMEN,M.V.A.S.NAVARRO,
REMARK 1 AUTH 2 M.H.RIDER,P.A.M.MICHELS,R.C.GARRATT,D.J.RIGDEN
REMARK 1 TITL THE CRYSTAL STRUCTURE OF TRYPANOSOMA BRUCEI ENOLASE:
REMARK 1 TITL 2 VISUALISATION OF THE INHIBITORY METAL BINDING SITE III AND
REMARK 1 TITL 3 POTENTIAL AS TARGET FOR SELECTIVE, IRREVERSIBLE INHIBITION
REMARK 1 REF J.MOL.BIOL. V. 331 653 2003
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 12899835
REMARK 1 DOI 10.1016/S0022-2836(03)00752-6
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 33851
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1780
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4700
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 237
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3281
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 257
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : 0.04000
REMARK 3 B12 (A**2) : 0.00000
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): 0.473
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.029
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3376 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4556 ; 1.487 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 436 ; 8.755 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 140 ;38.164 ;24.714
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 603 ;13.659 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;19.118 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 506 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2520 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1702 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2301 ; 0.296 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 239 ; 0.128 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.044 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 59 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.127 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.016 ; 0.200
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): 2232 ; 1.476 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3435 ; 2.098 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1323 ; 2.950 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1118 ; 4.393 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -1 A 429
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1960 34.6057 34.1204
REMARK 3 T TENSOR
REMARK 3 T11: -0.1064 T22: -0.0826
REMARK 3 T33: -0.0770 T12: 0.0188
REMARK 3 T13: 0.0025 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.1081 L22: 0.7807
REMARK 3 L33: 1.6273 L12: -0.1944
REMARK 3 L13: -0.1059 L23: 0.4786
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: -0.0426 S13: -0.1424
REMARK 3 S21: 0.0698 S22: 0.0640 S23: -0.1082
REMARK 3 S31: 0.1734 S32: 0.2067 S33: -0.0275
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 703 A 959
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6651 37.0273 34.8884
REMARK 3 T TENSOR
REMARK 3 T11: -0.0761 T22: -0.0388
REMARK 3 T33: -0.0320 T12: 0.0167
REMARK 3 T13: -0.0061 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.1786 L22: 1.2354
REMARK 3 L33: 1.5977 L12: -0.2006
REMARK 3 L13: -0.1250 L23: 0.4369
REMARK 3 S TENSOR
REMARK 3 S11: -0.0433 S12: -0.0727 S13: -0.0630
REMARK 3 S21: 0.0225 S22: 0.0744 S23: -0.0982
REMARK 3 S31: 0.0485 S32: 0.1986 S33: -0.0312
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2PU0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042773.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU ULTRAX 18
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35659
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 17.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.40300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 1OEP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % (W/V) PEG1000, 0.01 M ZNSO4 OR
REMARK 280 ZNCL2, AND 0.1 M MES, PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.60950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.60950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 37.47300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.38000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.47300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.38000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.60950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.47300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.38000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.60950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.47300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.38000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 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: DIMERIC
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 54.60950
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 GLY A -2
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 LYS A 253 CD LYS A 253 CE 0.160
REMARK 500 LYS A 253 CE LYS A 253 NZ 0.165
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 VAL A 58 51.09 36.27
REMARK 500 VAL A 72 -59.72 -121.97
REMARK 500 ASN A 159 178.91 179.25
REMARK 500 ALA A 212 66.76 -115.95
REMARK 500 ASP A 318 -76.62 -127.55
REMARK 500 VAL A 322 42.12 38.70
REMARK 500 ASN A 338 20.30 -140.17
REMARK 500 THR A 395 25.96 -141.88
REMARK 500 ARG A 400 125.86 82.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 157 GLY A 158 36.22
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 SER A 40 O
REMARK 620 2 SER A 40 OG 83.8
REMARK 620 3 PAH A 600 O2 174.6 90.8
REMARK 620 4 PAH A 600 O2P 93.8 93.1 85.8
REMARK 620 5 HOH A 938 O 91.0 83.7 89.0 173.9
REMARK 620 6 HOH A 941 O 87.9 170.6 97.5 91.9 92.0
REMARK 620 N 1 2 3 4 5
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 ASP A 243 OD2
REMARK 620 2 GLU A 291 OE2 88.1
REMARK 620 3 ASP A 318 OD2 176.2 90.6
REMARK 620 4 PAH A 600 O3 94.7 88.7 88.9
REMARK 620 5 HOH A 940 O 85.6 105.6 91.3 165.7
REMARK 620 N 1 2 3 4
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 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PAH A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OEP RELATED DB: PDB
REMARK 900 FIRST STRUCTURE OF THE T. BRUCEI ENOLASE
REMARK 900 RELATED ID: 2PTW RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SULPHATE AND ZN ION IN A METAL
REMARK 900 BINDING SITE IV
REMARK 900 RELATED ID: 2PTX RELATED DB: PDB
REMARK 900 CLOSED CONFORMATION OF THE T. BRUCEI ENOLASE COMPLEXED WITH SULPHATE
REMARK 900 RELATED ID: 2PTY RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PEP
REMARK 900 RELATED ID: 2PTZ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PAH, HIS156-OUT CONFORMATION
DBREF 2PU0 A 1 429 UNP Q38BV6 Q38BV6_9TRYP 1 429
SEQADV 2PU0 GLY A -2 UNP Q38BV6 EXPRESSION TAG
SEQADV 2PU0 SER A -1 UNP Q38BV6 EXPRESSION TAG
SEQADV 2PU0 HIS A 0 UNP Q38BV6 EXPRESSION TAG
SEQADV 2PU0 LYS A 28 UNP Q38BV6 ARG 28 ENGINEERED MUTATION
SEQRES 1 A 432 GLY SER HIS MET THR ILE GLN LYS VAL HIS GLY ARG GLU
SEQRES 2 A 432 VAL LEU ASP SER ARG GLY ASN PRO THR VAL GLU VAL GLU
SEQRES 3 A 432 VAL THR THR GLU LYS GLY VAL PHE ARG SER ALA VAL PRO
SEQRES 4 A 432 SER GLY ALA SER THR GLY VAL TYR GLU ALA CYS GLU LEU
SEQRES 5 A 432 ARG ASP GLY ASP LYS LYS ARG TYR VAL GLY LYS GLY CYS
SEQRES 6 A 432 LEU GLN ALA VAL LYS ASN VAL ASN GLU VAL ILE GLY PRO
SEQRES 7 A 432 ALA LEU ILE GLY ARG ASP GLU LEU LYS GLN GLU GLU LEU
SEQRES 8 A 432 ASP THR LEU MET LEU ARG LEU ASP GLY THR PRO ASN LYS
SEQRES 9 A 432 GLY LYS LEU GLY ALA ASN ALA ILE LEU GLY CYS SER MET
SEQRES 10 A 432 ALA ILE SER LYS ALA ALA ALA ALA ALA LYS GLY VAL PRO
SEQRES 11 A 432 LEU TYR ARG TYR LEU ALA SER LEU ALA GLY THR LYS GLU
SEQRES 12 A 432 LEU ARG LEU PRO VAL PRO CYS PHE ASN VAL ILE ASN GLY
SEQRES 13 A 432 GLY LYS HIS ALA GLY ASN ALA LEU PRO PHE GLN GLU PHE
SEQRES 14 A 432 MET ILE ALA PRO VAL LYS ALA THR SER PHE SER GLU ALA
SEQRES 15 A 432 LEU ARG MET GLY SER GLU VAL TYR HIS SER LEU ARG GLY
SEQRES 16 A 432 ILE ILE LYS LYS LYS TYR GLY GLN ASP ALA VAL ASN VAL
SEQRES 17 A 432 GLY ASP GLU GLY GLY PHE ALA PRO PRO ILE LYS ASP ILE
SEQRES 18 A 432 ASN GLU PRO LEU PRO ILE LEU MET GLU ALA ILE GLU GLU
SEQRES 19 A 432 ALA GLY HIS ARG GLY LYS PHE ALA ILE CYS MET ASP CYS
SEQRES 20 A 432 ALA ALA SER GLU THR TYR ASP GLU LYS LYS GLN GLN TYR
SEQRES 21 A 432 ASN LEU THR PHE LYS SER PRO GLU PRO THR TRP VAL THR
SEQRES 22 A 432 ALA GLU GLN LEU ARG GLU THR TYR CYS LYS TRP ALA HIS
SEQRES 23 A 432 ASP TYR PRO ILE VAL SER ILE GLU ASP PRO TYR ASP GLN
SEQRES 24 A 432 ASP ASP PHE ALA GLY PHE ALA GLY ILE THR GLU ALA LEU
SEQRES 25 A 432 LYS GLY LYS THR GLN ILE VAL GLY ASP ASP LEU THR VAL
SEQRES 26 A 432 THR ASN THR GLU ARG ILE LYS MET ALA ILE GLU LYS LYS
SEQRES 27 A 432 ALA CYS ASN SER LEU LEU LEU LYS ILE ASN GLN ILE GLY
SEQRES 28 A 432 THR ILE SER GLU ALA ILE ALA SER SER LYS LEU CYS MET
SEQRES 29 A 432 GLU ASN GLY TRP SER VAL MET VAL SER HIS ARG SER GLY
SEQRES 30 A 432 GLU THR GLU ASP THR TYR ILE ALA ASP LEU VAL VAL ALA
SEQRES 31 A 432 LEU GLY SER GLY GLN ILE LYS THR GLY ALA PRO CYS ARG
SEQRES 32 A 432 GLY GLU ARG THR ALA LYS LEU ASN GLN LEU LEU ARG ILE
SEQRES 33 A 432 GLU GLU GLU LEU GLY ALA HIS ALA LYS PHE GLY PHE PRO
SEQRES 34 A 432 GLY TRP SER
HET ZN A 501 1
HET ZN A 502 1
HET ZN A 505 1
HET PAH A 600 9
HET EDO A 700 4
HET EDO A 701 4
HET EDO A 702 4
HETNAM ZN ZINC ION
HETNAM PAH PHOSPHONOACETOHYDROXAMIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ZN 3(ZN 2+)
FORMUL 5 PAH C2 H6 N O5 P
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 9 HOH *257(H2 O)
HELIX 1 1 ARG A 56 LYS A 60 5 5
HELIX 2 2 CYS A 62 VAL A 72 1 11
HELIX 3 3 VAL A 72 ILE A 78 1 7
HELIX 4 4 LYS A 84 GLY A 97 1 14
HELIX 5 5 GLY A 105 GLY A 125 1 21
HELIX 6 6 PRO A 127 GLY A 137 1 11
HELIX 7 7 GLY A 154 ALA A 157 5 4
HELIX 8 8 SER A 175 GLY A 199 1 25
HELIX 9 9 GLN A 200 VAL A 203 5 4
HELIX 10 10 GLU A 220 ALA A 232 1 13
HELIX 11 11 ALA A 245 GLU A 248 5 4
HELIX 12 12 THR A 270 TYR A 285 1 16
HELIX 13 13 ASP A 298 LEU A 309 1 12
HELIX 14 14 ASN A 324 LYS A 334 1 11
HELIX 15 15 LYS A 343 GLY A 348 1 6
HELIX 16 16 THR A 349 ASN A 363 1 15
HELIX 17 17 THR A 379 GLY A 389 1 11
HELIX 18 18 ARG A 400 GLY A 418 1 19
HELIX 19 19 PHE A 425 SER A 429 5 5
SHEET 1 A 3 LYS A 5 LEU A 12 0
SHEET 2 A 3 PRO A 18 THR A 26 -1 O GLU A 23 N HIS A 7
SHEET 3 A 3 GLY A 29 ALA A 34 -1 O SER A 33 N VAL A 22
SHEET 1 B 2 ARG A 142 LEU A 143 0
SHEET 2 B 2 LYS A 422 PHE A 423 1 O LYS A 422 N LEU A 143
SHEET 1 C 9 VAL A 145 PRO A 146 0
SHEET 2 C 9 GLN A 392 LYS A 394 1 O ILE A 393 N VAL A 145
SHEET 3 C 9 SER A 366 SER A 370 1 N VAL A 369 O LYS A 394
SHEET 4 C 9 SER A 339 LEU A 342 1 N LEU A 340 O MET A 368
SHEET 5 C 9 GLN A 314 GLY A 317 1 N GLY A 317 O SER A 339
SHEET 6 C 9 ILE A 287 GLU A 291 1 N ILE A 290 O GLN A 314
SHEET 7 C 9 ALA A 239 ASP A 243 1 N MET A 242 O SER A 289
SHEET 8 C 9 GLU A 165 ALA A 169 -1 N MET A 167 O CYS A 241
SHEET 9 C 9 PHE A 148 ASN A 152 -1 N PHE A 148 O ILE A 168
SHEET 1 D 3 TYR A 250 ASP A 251 0
SHEET 2 D 3 GLN A 256 ASN A 258 -1 O GLN A 256 N ASP A 251
SHEET 3 D 3 TRP A 268 VAL A 269 -1 O VAL A 269 N TYR A 257
LINK OE2 GLU A 27 ZN ZN A 505 1555 1555 1.96
LINK O SER A 40 ZN ZN A 502 1555 1555 2.13
LINK OG SER A 40 ZN ZN A 502 1555 1555 2.24
LINK OD2 ASP A 243 ZN ZN A 501 1555 1555 2.18
LINK OE2 GLU A 291 ZN ZN A 501 1555 1555 2.00
LINK OD2 ASP A 318 ZN ZN A 501 1555 1555 2.17
LINK ZN ZN A 501 O3 PAH A 600 1555 1555 2.04
LINK ZN ZN A 501 O HOH A 940 1555 1555 2.03
LINK ZN ZN A 502 O2 PAH A 600 1555 1555 2.24
LINK ZN ZN A 502 O2P PAH A 600 1555 1555 2.14
LINK ZN ZN A 502 O HOH A 938 1555 1555 2.17
LINK ZN ZN A 502 O HOH A 941 1555 1555 2.18
SITE 1 AC1 5 ASP A 243 GLU A 291 ASP A 318 PAH A 600
SITE 2 AC1 5 HOH A 940
SITE 1 AC2 4 SER A 40 PAH A 600 HOH A 938 HOH A 941
SITE 1 AC3 4 HIS A 0 GLU A 27 HIS A 283 HOH A 939
SITE 1 AC4 18 GLY A 38 ALA A 39 SER A 40 HIS A 156
SITE 2 AC4 18 GLN A 164 GLU A 165 ASP A 243 GLU A 291
SITE 3 AC4 18 ASP A 318 LEU A 341 LYS A 343 ARG A 372
SITE 4 AC4 18 SER A 373 LYS A 394 ZN A 501 ZN A 502
SITE 5 AC4 18 HOH A 938 HOH A 955
SITE 1 AC5 4 TYR A 129 GLN A 409 GLU A 416 HOH A 752
SITE 1 AC6 7 ARG A 9 GLU A 10 LEU A 411 GLU A 415
SITE 2 AC6 7 HOH A 763 HOH A 788 HOH A 918
SITE 1 AC7 4 ARG A 142 GLY A 389 SER A 390 PRO A 426
CRYST1 74.946 110.760 109.219 90.00 90.00 90.00 C 2 2 21 8
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 0.013343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009156 0.00000
(ATOM LINES ARE NOT SHOWN.)
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