HEADER TRANSFERASE 30-AUG-04 1W77
TITLE 2C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE (ISPD) FROM
TITLE 2 ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYTIDYLTRANSFERASE DOMAIN, RESIDUES 76-302;
COMPND 5 SYNONYM: 4-DIPHOSPHOCYTIDYL-2C-METHYL-D-ERYTHRITOL SYNTHASE, PUTATIVE
COMPND 6 SUGAR NUCLEOTIDE PHOSPHORYLASE;
COMPND 7 EC: 2.7.7.60;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: CHLOROPLAST TARGETING SEQUENCE REMOVED, COMPOUND
COMPND 11 STARTS AT RESIDUE 75
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15(PREP4);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNCO113
KEYWDS PLANTHERBICIDE, CYTIDYLYLTRANSFERASE, ARABIDOPSIS THALIANA, NON-
KEYWDS 2 MEVALONATE PATHWAY, ISOPRENOID, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GABRIELSEN,J.KAISER,F.ROHDICH,W.EISENREICH,A.BACHER,C.S.BOND,
AUTHOR 2 W.N.HUNTER
REVDAT 3 13-DEC-23 1W77 1 LINK
REVDAT 2 24-FEB-09 1W77 1 VERSN
REVDAT 1 21-FEB-06 1W77 0
JRNL AUTH M.GABRIELSEN,J.KAISER,F.ROHDICH,W.EISENREICH,R.LAUPITZ,
JRNL AUTH 2 A.BACHER,C.S.BOND,W.N.HUNTER
JRNL TITL THE CRYSTAL STRUCTURE OF A PLANT 2C-METHYL-D-ERYTHRITOL
JRNL TITL 2 4-PHOSPHATE CYTIDYLYLTRANSFERASE EXHIBITS A DISTINCT
JRNL TITL 3 QUATERNARY STRUCTURE COMPARED TO BACTERIAL HOMOLOGUES AND A
JRNL TITL 4 POSSIBLE ROLE IN FEEDBACK REGULATION FOR CYTIDINE
JRNL TITL 5 MONOPHOSPHATE.
JRNL REF FEBS J. V. 273 1065 2006
JRNL REFN ISSN 1742-464X
JRNL PMID 16478479
JRNL DOI 10.1111/J.1742-4658.2006.05133.X
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 15674
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.349
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 833
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1091
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.4170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1640
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.02000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.222
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.244
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.208
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.459
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1689 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2295 ; 1.652 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 208 ; 9.782 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 68 ;32.588 ;25.882
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 294 ;21.323 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;21.091 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 276 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1228 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 888 ; 0.298 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1135 ; 0.330 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 151 ; 0.299 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 89 ; 0.324 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.269 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1083 ; 9.567 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1723 ;11.302 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 675 ;16.556 ;10.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 572 ;18.780 ;10.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1W77 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1290020919.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-03
REMARK 200 TEMPERATURE (KELVIN) : 160.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393
REMARK 200 MONOCHROMATOR : SI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16508
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 29.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 16.90
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.3000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BEAST
REMARK 200 STARTING MODEL: PDB ENTRY 1I52
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 0.05 M CADMIUM
REMARK 280 SULFATE, 1 M SODIUM ACETATE, 0.04 COPPER(II) CHLORIDE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 37.24800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 21.50514
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 74.34200
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 37.24800
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 21.50514
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 74.34200
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 37.24800
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 21.50514
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 74.34200
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 37.24800
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 21.50514
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 74.34200
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 37.24800
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 21.50514
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 74.34200
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 37.24800
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 21.50514
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 74.34200
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 43.01029
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 148.68400
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 43.01029
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 148.68400
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 43.01029
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 148.68400
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 43.01029
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 148.68400
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 43.01029
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 148.68400
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 43.01029
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 148.68400
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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 -0.500000 -0.866025 0.000000 74.49600
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 43.01029
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -74.34200
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION LYS 75 MET
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 GLN A 88
REMARK 465 GLY A 89
REMARK 465 LYS A 90
REMARK 465 ARG A 91
REMARK 465 MET A 92
REMARK 465 LYS A 93
REMARK 465 MET A 94
REMARK 465 LYS A 224
REMARK 465 THR A 225
REMARK 465 LEU A 226
REMARK 465 ASP A 227
REMARK 465 ARG A 228
REMARK 465 LYS A 229
REMARK 465 ASP A 261
REMARK 465 ASP A 301
REMARK 465 SER A 302
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 LYS A 155 CG CD CE NZ
REMARK 470 LEU A 257 CG CD1 CD2
REMARK 470 LEU A 292 CG CD1 CD2
REMARK 470 ARG A 296 CG CD NE CZ NH1 NH2
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 N LYS A 270 O HOH A 2148 1.68
REMARK 500 OE1 GLU A 138 OE1 GLU A 141 1.72
REMARK 500 OD1 ASN A 171 O HOH A 2063 1.85
REMARK 500 O HOH A 2146 O HOH A 2149 1.98
REMARK 500 O TYR A 162 NE2 GLN A 166 2.11
REMARK 500 O HOH A 2050 O HOH A 2102 2.15
REMARK 500 O HOH A 2044 O HOH A 2084 2.15
REMARK 500 OD2 ASP A 169 O HOH A 2061 2.16
REMARK 500 OG SER A 220 O HOH A 2119 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2087 O HOH A 2149 2665 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 169 CB ASP A 169 CG 0.147
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 130 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 147 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 159 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 169 CB - CG - OD2 ANGL. DEV. = 12.6 DEGREES
REMARK 500 ASP A 189 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 290 CB - CG - OD2 ANGL. DEV. = 5.7 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 ILE A 101 124.69 -39.55
REMARK 500 LEU A 104 -84.53 56.84
REMARK 500 PHE A 132 -32.63 -34.91
REMARK 500 SER A 143 41.04 -91.54
REMARK 500 SER A 180 -37.21 -38.91
REMARK 500 GLN A 235 -153.95 -119.72
REMARK 500 GLU A 255 -114.17 -90.50
REMARK 500 LEU A 257 123.69 108.67
REMARK 500 TYR A 268 -8.46 -49.27
REMARK 500 LYS A 270 -24.69 80.70
REMARK 500 THR A 286 -72.20 -130.85
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 ASP A 262 VAL A 263 135.96
REMARK 500 VAL A 263 SER A 264 126.64
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 A2029 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A2030 DISTANCE = 8.33 ANGSTROMS
REMARK 525 HOH A2031 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A2034 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH A2042 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A2047 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH A2060 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A2080 DISTANCE = 6.89 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 CD A1000 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 121 OE2
REMARK 620 2 GLU A 121 OE1 53.6
REMARK 620 3 GLU A 191 OE1 79.0 87.3
REMARK 620 4 GLU A 191 OE2 123.2 93.3 51.7
REMARK 620 5 HIS A 271 ND1 92.3 145.2 78.6 102.1
REMARK 620 6 HOH A2025 O 115.7 99.5 165.1 114.2 102.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A1002 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 138 OE2
REMARK 620 2 GLU A 138 OE1 70.7
REMARK 620 3 GLU A 141 OE1 91.9 58.8
REMARK 620 4 ASP A 169 OD1 85.2 133.5 164.4
REMARK 620 5 ASP A 169 OD2 126.4 150.2 93.9 75.7
REMARK 620 6 HOH A2061 O 173.9 106.3 90.9 93.5 58.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A1001 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 167 OE2
REMARK 620 2 GLU A 167 OE2 77.1
REMARK 620 3 GLU A 167 OE1 106.9 70.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A1004 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 290 OD2
REMARK 620 2 ASP A 290 OD1 49.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C5P A3001
DBREF 1W77 A 75 302 UNP O64726 O64726 75 302
SEQADV 1W77 MET A 75 UNP O64726 LYS 75 ENGINEERED MUTATION
SEQRES 1 A 228 MET GLU LYS SER VAL SER VAL ILE LEU LEU ALA GLY GLY
SEQRES 2 A 228 GLN GLY LYS ARG MET LYS MET SER MET PRO LYS GLN TYR
SEQRES 3 A 228 ILE PRO LEU LEU GLY GLN PRO ILE ALA LEU TYR SER PHE
SEQRES 4 A 228 PHE THR PHE SER ARG MET PRO GLU VAL LYS GLU ILE VAL
SEQRES 5 A 228 VAL VAL CYS ASP PRO PHE PHE ARG ASP ILE PHE GLU GLU
SEQRES 6 A 228 TYR GLU GLU SER ILE ASP VAL ASP LEU ARG PHE ALA ILE
SEQRES 7 A 228 PRO GLY LYS GLU ARG GLN ASP SER VAL TYR SER GLY LEU
SEQRES 8 A 228 GLN GLU ILE ASP VAL ASN SER GLU LEU VAL CYS ILE HIS
SEQRES 9 A 228 ASP SER ALA ARG PRO LEU VAL ASN THR GLU ASP VAL GLU
SEQRES 10 A 228 LYS VAL LEU LYS ASP GLY SER ALA VAL GLY ALA ALA VAL
SEQRES 11 A 228 LEU GLY VAL PRO ALA LYS ALA THR ILE LYS GLU VAL ASN
SEQRES 12 A 228 SER ASP SER LEU VAL VAL LYS THR LEU ASP ARG LYS THR
SEQRES 13 A 228 LEU TRP GLU MET GLN THR PRO GLN VAL ILE LYS PRO GLU
SEQRES 14 A 228 LEU LEU LYS LYS GLY PHE GLU LEU VAL LYS SER GLU GLY
SEQRES 15 A 228 LEU GLU VAL THR ASP ASP VAL SER ILE VAL GLU TYR LEU
SEQRES 16 A 228 LYS HIS PRO VAL TYR VAL SER GLN GLY SER TYR THR ASN
SEQRES 17 A 228 ILE LYS VAL THR THR PRO ASP ASP LEU LEU LEU ALA GLU
SEQRES 18 A 228 ARG ILE LEU SER GLU ASP SER
HET CD A1000 1
HET CU A1001 1
HET CU A1002 1
HET CU A1003 1
HET CU A1004 1
HET C5P A3001 21
HETNAM CD CADMIUM ION
HETNAM CU COPPER (II) ION
HETNAM C5P CYTIDINE-5'-MONOPHOSPHATE
FORMUL 2 CD CD 2+
FORMUL 3 CU 4(CU 2+)
FORMUL 7 C5P C9 H14 N3 O8 P
FORMUL 8 HOH *166(H2 O)
HELIX 1 1 ILE A 108 ARG A 118 1 11
HELIX 2 2 ASP A 130 PHE A 133 5 4
HELIX 3 3 ARG A 134 GLU A 139 1 6
HELIX 4 4 GLU A 156 GLU A 167 1 12
HELIX 5 5 ASN A 186 GLY A 201 1 16
HELIX 6 6 LYS A 241 GLU A 255 1 15
HELIX 7 7 VAL A 266 LYS A 270 5 5
HELIX 8 8 THR A 287 GLU A 300 1 14
SHEET 1 AA 7 ASP A 147 ALA A 151 0
SHEET 2 AA 7 VAL A 122 VAL A 128 1 O LYS A 123 N ASP A 147
SHEET 3 AA 7 VAL A 79 LEU A 84 1 O VAL A 79 N LYS A 123
SHEET 4 AA 7 LEU A 174 ASP A 179 1 O LEU A 174 N SER A 80
SHEET 5 AA 7 TRP A 232 ILE A 240 -1 O GLN A 238 N ILE A 177
SHEET 6 AA 7 ALA A 202 PRO A 208 -1 O ALA A 203 N VAL A 239
SHEET 7 AA 7 TYR A 274 GLN A 277 1 O TYR A 274 N VAL A 204
SHEET 1 AB 2 PRO A 102 LEU A 103 0
SHEET 2 AB 2 GLN A 106 PRO A 107 -1 O GLN A 106 N LEU A 103
LINK OE2 GLU A 121 CD CD A1000 1555 1555 1.79
LINK OE1 GLU A 121 CD CD A1000 1555 1555 2.70
LINK OE2 GLU A 138 CU CU A1002 1555 1555 2.19
LINK OE1 GLU A 138 CU CU A1002 1555 1555 1.44
LINK OE1 GLU A 141 CU CU A1002 1555 1555 1.95
LINK OE2 GLU A 167 CU CU A1001 1555 1555 2.43
LINK OE2 GLU A 167 CU CU A1001 5675 1555 1.70
LINK OE1 GLU A 167 CU CU A1001 5675 1555 2.02
LINK OD1 ASP A 169 CU CU A1002 5675 1555 1.89
LINK OD2 ASP A 169 CU CU A1002 5675 1555 1.66
LINK OE1 GLU A 191 CD CD A1000 1555 1555 2.63
LINK OE2 GLU A 191 CD CD A1000 1555 1555 2.39
LINK ND1 HIS A 271 CD CD A1000 2665 1555 2.31
LINK OD2 ASP A 290 CU CU A1004 1555 1555 2.33
LINK OD1 ASP A 290 CU CU A1004 1555 1555 2.75
LINK CD CD A1000 O HOH A2025 1555 1555 2.46
LINK CU CU A1002 O HOH A2061 1555 5675 2.49
CISPEP 1 THR A 236 PRO A 237 0 13.31
SITE 1 AC1 4 GLU A 121 GLU A 191 HIS A 271 HOH A2025
SITE 1 AC2 1 GLU A 167
SITE 1 AC3 4 GLU A 138 GLU A 141 ASP A 169 HOH A2061
SITE 1 AC4 1 HOH A2162
SITE 1 AC5 2 THR A 286 ASP A 290
SITE 1 AC6 11 LEU A 84 ALA A 85 GLY A 86 GLY A 87
SITE 2 AC6 11 GLY A 154 LYS A 155 GLU A 156 SER A 160
SITE 3 AC6 11 ASP A 179 LYS A 284 HOH A2166
CRYST1 74.496 74.496 223.026 90.00 90.00 120.00 H 3 2 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 0.013424 0.007750 0.000000 0.00000
SCALE2 0.000000 0.015500 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004484 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
