HEADER TRANSFERASE 28-JUN-10 3NPM
TITLE CRYSTAL STRUCTURE OF THE C47A/A241C DISULFIDE-LINKED C6 ASPARTATE
TITLE 2 TRANSCARBAMOYLASE ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.1.3.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: PYRB, B4245, JW4204;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: EK1104;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEK613
KEYWDS ASPARTATE TRANSCARBAMOYLASE, DISULFIDE BOND, PHOSPHATE, CATALYSIS,
KEYWDS 2 PRODUCT RELEASE, COOPERATIVITY, ALLOSTERY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.MENDES,E.R.KANTROWITZ
REVDAT 2 06-SEP-23 3NPM 1 REMARK SEQADV
REVDAT 1 11-MAY-11 3NPM 0
JRNL AUTH K.R.MENDES,E.R.KANTROWITZ
JRNL TITL A COOPERATIVE ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE
JRNL TITL 2 WITHOUT REGULATORY SUBUNITS .
JRNL REF BIOCHEMISTRY V. 49 7694 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20681545
JRNL DOI 10.1021/BI1010333
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 28888
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1469
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 42.7571 - 4.5283 1.00 2971 160 0.2237 0.2388
REMARK 3 2 4.5283 - 3.5948 1.00 2804 139 0.1590 0.1756
REMARK 3 3 3.5948 - 3.1405 1.00 2758 146 0.1629 0.1942
REMARK 3 4 3.1405 - 2.8535 1.00 2731 142 0.1665 0.1794
REMARK 3 5 2.8535 - 2.6490 1.00 2707 161 0.1561 0.1877
REMARK 3 6 2.6490 - 2.4928 1.00 2718 141 0.1558 0.2222
REMARK 3 7 2.4928 - 2.3680 1.00 2684 138 0.1593 0.1867
REMARK 3 8 2.3680 - 2.2649 1.00 2697 155 0.1656 0.1885
REMARK 3 9 2.2649 - 2.1777 1.00 2677 136 0.1823 0.2346
REMARK 3 10 2.1777 - 2.1026 1.00 2672 151 0.1602 0.2050
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 77.62
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 2449
REMARK 3 ANGLE : 0.916 3324
REMARK 3 CHIRALITY : 0.063 383
REMARK 3 PLANARITY : 0.004 430
REMARK 3 DIHEDRAL : 17.182 888
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NPM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000060121.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : FIBER-OPTIC TAPER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28904
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 22.80
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 43.00
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
REMARK 200 R SYM FOR SHELL (I) : 0.54100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 1D09
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML OF C47A/A241C C6 IN 100 MM
REMARK 280 TRIS-ACETATE PH 8.3, IN A 1:1 RATIO (V/V), WITH RESERVOIR.
REMARK 280 CRYSTALLIZATION BUFFER CONSISTED OF 40% PEG 1000, 100 MM
REMARK 280 NH4H2PO4, AND 100 MM HEPES, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
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 Y+1/4,X+3/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
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 70.89000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.89000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.89000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.89000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.89000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.89000
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 70.89000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.89000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.89000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.89000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.89000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.89000
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 70.89000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.89000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.89000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.89000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.89000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.89000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 35.44500
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 106.33500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 106.33500
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 35.44500
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 35.44500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 35.44500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 106.33500
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 106.33500
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 35.44500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 106.33500
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 35.44500
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 106.33500
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 35.44500
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 106.33500
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 106.33500
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 106.33500
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 35.44500
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 106.33500
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 35.44500
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 35.44500
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 35.44500
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 106.33500
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 106.33500
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 35.44500
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 35.44500
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 106.33500
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 106.33500
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 106.33500
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 106.33500
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 35.44500
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 106.33500
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 35.44500
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 106.33500
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 35.44500
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 35.44500
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 35.44500
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -180.0 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 BIOMT1 2 0.000000 0.000000 1.000000 70.89000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 70.89000
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 70.89000
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 -70.89000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 35.44500
REMARK 350 BIOMT2 4 1.000000 0.000000 0.000000 -35.44500
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -35.44500
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 106.33500
REMARK 350 BIOMT2 5 0.000000 0.000000 1.000000 35.44500
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 -35.44500
REMARK 350 BIOMT1 6 0.000000 0.000000 -1.000000 35.44500
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 35.44500
REMARK 350 BIOMT3 6 -1.000000 0.000000 0.000000 35.44500
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 1
REMARK 465 VAL A 309
REMARK 465 LEU A 310
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 GLU A 147 CD GLU A 147 OE2 0.083
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 THR A 53 -64.71 -109.99
REMARK 500 ASN A 132 -84.92 -84.14
REMARK 500 LEU A 267 158.08 66.73
REMARK 500 VAL A 270 -91.31 -115.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 312
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MPU RELATED DB: PDB
REMARK 900 C47A/A241C DISULFIDE-LINKED HOLOENZYME COMPLEXED WITH PHOSPHATE
REMARK 900 RELATED ID: 1D09 RELATED DB: PDB
REMARK 900 WILD-TYPE PROTEIN COMPLEXED WITH PALA
REMARK 900 RELATED ID: 2A0F RELATED DB: PDB
REMARK 900 D236A HOLOENZYME COMPLEXED WITH PAM
DBREF 3NPM A 1 310 UNP P0A786 PYRB_ECOLI 2 311
SEQADV 3NPM ALA A 47 UNP P0A786 CYS 48 ENGINEERED MUTATION
SEQADV 3NPM CYS A 241 UNP P0A786 ALA 242 ENGINEERED MUTATION
SEQRES 1 A 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN
SEQRES 2 A 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR
SEQRES 3 A 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU
SEQRES 4 A 310 LYS HIS LYS VAL ILE ALA SER ALA PHE PHE GLU ALA SER
SEQRES 5 A 310 THR ARG THR ARG LEU SER PHE GLU THR SER MET HIS ARG
SEQRES 6 A 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN
SEQRES 7 A 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR
SEQRES 8 A 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET
SEQRES 9 A 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU
SEQRES 10 A 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY
SEQRES 11 A 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE
SEQRES 12 A 310 THR ILE GLN GLU THR GLN GLY ARG LEU ASP ASN LEU HIS
SEQRES 13 A 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL
SEQRES 14 A 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN
SEQRES 15 A 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO
SEQRES 16 A 310 GLN TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA
SEQRES 17 A 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU
SEQRES 18 A 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG
SEQRES 19 A 310 LEU ASP PRO SER GLU TYR CYS ASN VAL LYS ALA GLN PHE
SEQRES 20 A 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN
SEQRES 21 A 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE
SEQRES 22 A 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE
SEQRES 23 A 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU
SEQRES 24 A 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU
HET PO4 A 311 5
HET PO4 A 312 5
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 HOH *222(H2 O)
HELIX 1 1 SER A 11 LEU A 15 5 5
HELIX 2 2 SER A 16 ASN A 33 1 18
HELIX 3 3 THR A 53 LEU A 66 1 14
HELIX 4 4 ASP A 75 ASN A 78 5 4
HELIX 5 5 THR A 79 LYS A 84 1 6
HELIX 6 6 THR A 87 SER A 96 1 10
HELIX 7 7 GLY A 110 GLU A 117 1 8
HELIX 8 8 HIS A 134 GLY A 150 1 17
HELIX 9 9 GLY A 166 ALA A 177 1 12
HELIX 10 10 PRO A 189 ALA A 193 5 5
HELIX 11 11 PRO A 195 LYS A 205 1 11
HELIX 12 12 ILE A 215 ALA A 220 1 6
HELIX 13 13 GLN A 231 LEU A 235 5 5
HELIX 14 14 ASP A 236 VAL A 243 5 8
HELIX 15 15 ARG A 250 HIS A 255 5 6
HELIX 16 16 ALA A 274 THR A 280 5 7
HELIX 17 17 TRP A 284 ASN A 305 1 22
SHEET 1 A 4 SER A 69 PHE A 73 0
SHEET 2 A 4 VAL A 43 PHE A 48 1 N SER A 46 O VAL A 71
SHEET 3 A 4 ALA A 101 HIS A 106 1 O VAL A 103 N ALA A 47
SHEET 4 A 4 VAL A 124 ASP A 129 1 O LEU A 125 N ILE A 102
SHEET 1 B 5 TRP A 209 LEU A 211 0
SHEET 2 B 5 ARG A 183 ILE A 187 1 N PHE A 186 O SER A 210
SHEET 3 B 5 HIS A 156 VAL A 160 1 N VAL A 157 O ARG A 183
SHEET 4 B 5 ILE A 224 MET A 227 1 O TYR A 226 N ALA A 158
SHEET 5 B 5 LYS A 262 LEU A 264 1 O LEU A 264 N MET A 227
CISPEP 1 LEU A 267 PRO A 268 0 -1.06
SITE 1 AC1 10 SER A 52 THR A 53 ARG A 54 THR A 55
SITE 2 AC1 10 SER A 80 LYS A 84 ARG A 105 LEU A 267
SITE 3 AC1 10 PO4 A 312 HOH A 493
SITE 1 AC2 11 THR A 55 LYS A 84 ARG A 105 HIS A 134
SITE 2 AC2 11 ARG A 167 THR A 168 LEU A 267 PO4 A 311
SITE 3 AC2 11 HOH A 330 HOH A 332 HOH A 493
CRYST1 141.780 141.780 141.780 90.00 90.00 90.00 P 43 3 2 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 0.007053 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007053 0.00000
(ATOM LINES ARE NOT SHOWN.)
END