HEADER LIGASE 09-SEP-07 2R7N
TITLE CRYSTAL STRUCTURE OF FAICAR SYNTHETASE (PURP) FROM M. JANNASCHII
TITLE 2 COMPLEXED WITH ADP AND FAICAR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5-FORMAMINOIMIDAZOLE-4-CARBOXAMIDE-1-(BETA)-D-RIBOFURANOSYL
COMPND 3 5'-MONOPHOSPHATE SYNTHETASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: 5-AMINOIMIDAZOLE-4-CARBOXAMIDE-1-BETA-D-RIBOFURANOSYL 5'-
COMPND 6 MONOPHOSPHATE-FORMATE LIGASE;
COMPND 7 EC: 6.3.4.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 2190;
SOURCE 4 GENE: PURP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET19
KEYWDS ATP-GRASP SUPERFAMILY, ATP-BINDING, LIGASE, MAGNESIUM, MANGANESE,
KEYWDS 2 METAL-BINDING, NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,R.H.WHITE,S.E.EALICK
REVDAT 5 21-FEB-24 2R7N 1 REMARK
REVDAT 4 25-OCT-17 2R7N 1 REMARK
REVDAT 3 24-FEB-09 2R7N 1 VERSN
REVDAT 2 22-JUL-08 2R7N 1 JRNL
REVDAT 1 04-DEC-07 2R7N 0
JRNL AUTH Y.ZHANG,R.H.WHITE,S.E.EALICK
JRNL TITL CRYSTAL STRUCTURE AND FUNCTION OF
JRNL TITL 2 5-FORMAMINOIMIDAZOLE-4-CARBOXAMIDE RIBONUCLEOTIDE SYNTHETASE
JRNL TITL 3 FROM METHANOCALDOCOCCUS JANNASCHII.
JRNL REF BIOCHEMISTRY V. 47 205 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18069798
JRNL DOI 10.1021/BI701406G
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 20891
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1069
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 859
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2827
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 58
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.66000
REMARK 3 B22 (A**2) : 2.66000
REMARK 3 B33 (A**2) : -3.99000
REMARK 3 B12 (A**2) : 1.33000
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): 0.322
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.271
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.175
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.365
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2937 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3966 ; 1.125 ; 2.007
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 353 ; 5.467 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;36.228 ;24.697
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 540 ;14.921 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;18.632 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 439 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2173 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1513 ; 0.239 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2049 ; 0.329 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 273 ; 0.225 ; 0.500
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): 130 ; 0.203 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.284 ; 0.500
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): 1807 ; 5.696 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2869 ; 7.843 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1248 ; 6.010 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1097 ; 7.808 ; 3.000
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 : 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 2R7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20891
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 92.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.23400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 64.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M (NH4)2SO4, 0.2 M NACL, 0.1 M NA
REMARK 280 ACETATE, PH 4.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 54.00050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 31.17720
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 84.75833
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 54.00050
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 31.17720
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 84.75833
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 54.00050
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 31.17720
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 84.75833
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 54.00050
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 31.17720
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 84.75833
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 54.00050
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 31.17720
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 84.75833
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 54.00050
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 31.17720
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 84.75833
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 62.35441
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 169.51667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 62.35441
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 169.51667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 62.35441
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 169.51667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 62.35441
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 169.51667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 62.35441
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 169.51667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 62.35441
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 169.51667
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 300 REMARK: BIOLOGICAL UNIT IS A HEXAMER FROM THE MONOMER IN THE
REMARK 300 ASYMMETRIC UNIT BY THE OPERATIONS: (X,Y,Z), (-Y,X-Y,Z), (-X+Y,-X,Z),
REMARK 300 (Y,X,-Z), (X-Y,-Y,-Z), (-X,-X+Y,-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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 37030 ANGSTROM**2
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 0.00000
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 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 614 LIES ON A SPECIAL POSITION.
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 PRO A 158
REMARK 465 GLY A 159
REMARK 465 ALA A 160
REMARK 465 ARG A 161
REMARK 465 GLY A 162
REMARK 465 GLY A 163
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 ARG A 164 CG CD NE CZ NH1 NH2
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 HIS A 92 CA HIS A 92 CB -0.155
REMARK 500 HIS A 92 C HIS A 92 O -0.142
REMARK 500 GLY A 93 C GLY A 93 O -0.178
REMARK 500 SER A 94 CB SER A 94 OG -0.089
REMARK 500 SER A 94 C SER A 94 O -0.120
REMARK 500 PHE A 95 CG PHE A 95 CD2 -0.126
REMARK 500 PHE A 95 CG PHE A 95 CD1 -0.094
REMARK 500 PHE A 95 CD1 PHE A 95 CE1 -0.238
REMARK 500 PHE A 95 CE1 PHE A 95 CZ -0.195
REMARK 500 PHE A 95 CZ PHE A 95 CE2 -0.165
REMARK 500 PHE A 95 CE2 PHE A 95 CD2 -0.266
REMARK 500 PHE A 95 C PHE A 95 O -0.151
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 2 122.27 -34.79
REMARK 500 LYS A 13 2.17 -68.21
REMARK 500 ASN A 15 97.86 -64.67
REMARK 500 SER A 26 170.53 176.99
REMARK 500 HIS A 27 -76.54 75.60
REMARK 500 ASN A 106 -3.49 -150.70
REMARK 500 TRP A 121 3.70 -56.09
REMARK 500 LYS A 184 6.60 -64.70
REMARK 500 ASP A 218 62.99 38.92
REMARK 500 SER A 266 -4.05 -59.73
REMARK 500 ARG A 314 -160.74 -107.66
REMARK 500 MET A 355 29.92 -143.07
REMARK 500 ILE A 359 -10.09 -140.28
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 SO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAI A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R7K RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH AMPPCP AND AICAR
REMARK 900 RELATED ID: 2R7L RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH ATP AND AICAR
REMARK 900 RELATED ID: 2R7M RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH AMP
DBREF 2R7N A 1 361 UNP Q57600 PURP_METJA 1 361
SEQRES 1 A 361 MET ILE SER LYS ASP GLU ILE LEU GLU ILE PHE ASP LYS
SEQRES 2 A 361 TYR ASN LYS ASP GLU ILE THR ILE ALA THR LEU GLY SER
SEQRES 3 A 361 HIS THR SER LEU HIS ILE LEU LYS GLY ALA LYS LEU GLU
SEQRES 4 A 361 GLY PHE SER THR VAL CYS ILE THR MET LYS GLY ARG ASP
SEQRES 5 A 361 VAL PRO TYR LYS ARG PHE LYS VAL ALA ASP LYS PHE ILE
SEQRES 6 A 361 TYR VAL ASP ASN PHE SER ASP ILE LYS ASN GLU GLU ILE
SEQRES 7 A 361 GLN GLU LYS LEU ARG GLU LEU ASN SER ILE VAL VAL PRO
SEQRES 8 A 361 HIS GLY SER PHE ILE ALA TYR CYS GLY LEU ASP ASN VAL
SEQRES 9 A 361 GLU ASN SER PHE LEU VAL PRO MET PHE GLY ASN ARG ARG
SEQRES 10 A 361 ILE LEU ARG TRP GLU SER GLU ARG SER LEU GLU GLY LYS
SEQRES 11 A 361 LEU LEU ARG GLU ALA GLY LEU ARG VAL PRO LYS LYS TYR
SEQRES 12 A 361 GLU SER PRO GLU ASP ILE ASP GLY THR VAL ILE VAL LYS
SEQRES 13 A 361 PHE PRO GLY ALA ARG GLY GLY ARG GLY TYR PHE ILE ALA
SEQRES 14 A 361 SER SER THR GLU GLU PHE TYR LYS LYS ALA GLU ASP LEU
SEQRES 15 A 361 LYS LYS ARG GLY ILE LEU THR ASP GLU ASP ILE ALA ASN
SEQRES 16 A 361 ALA HIS ILE GLU GLU TYR VAL VAL GLY THR ASN PHE CYS
SEQRES 17 A 361 ILE HIS TYR PHE TYR SER PRO LEU LYS ASP GLU VAL GLU
SEQRES 18 A 361 LEU LEU GLY MET ASP LYS ARG TYR GLU SER ASN ILE ASP
SEQRES 19 A 361 GLY LEU VAL ARG ILE PRO ALA LYS ASP GLN LEU GLU MET
SEQRES 20 A 361 ASN ILE ASN PRO SER TYR VAL ILE THR GLY ASN ILE PRO
SEQRES 21 A 361 VAL VAL ILE ARG GLU SER LEU LEU PRO GLN VAL PHE GLU
SEQRES 22 A 361 MET GLY ASP LYS LEU VAL ALA LYS ALA LYS GLU LEU VAL
SEQRES 23 A 361 PRO PRO GLY MET ILE GLY PRO PHE CYS LEU GLN SER LEU
SEQRES 24 A 361 CYS ASN GLU ASN LEU GLU LEU VAL VAL PHE GLU MET SER
SEQRES 25 A 361 ALA ARG VAL ASP GLY GLY THR ASN SER PHE MET ASN GLY
SEQRES 26 A 361 GLY PRO TYR SER PHE LEU TYR ASN GLY GLU PRO LEU SER
SEQRES 27 A 361 MET GLY GLN ARG ILE ALA ARG GLU ILE LYS MET ALA LEU
SEQRES 28 A 361 GLN LEU ASP MET ILE ASP LYS ILE ILE SER
HET SO4 A 500 5
HET CL A 602 1
HET ADP A 400 27
HET FAI A 401 24
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM FAI 5-(FORMYLAMINO)-1-(5-O-PHOSPHONO-BETA-D-RIBOFURANOSYL)-
HETNAM 2 FAI 1H-IMIDAZOLE-4-CARBOXAMIDE
FORMUL 2 SO4 O4 S 2-
FORMUL 3 CL CL 1-
FORMUL 4 ADP C10 H15 N5 O10 P2
FORMUL 5 FAI C10 H15 N4 O9 P
FORMUL 6 HOH *58(H2 O)
HELIX 1 1 SER A 3 LYS A 13 1 11
HELIX 2 2 THR A 28 GLU A 39 1 12
HELIX 3 3 ASP A 52 PHE A 58 1 7
HELIX 4 4 ASN A 69 LYS A 74 5 6
HELIX 5 5 ASN A 75 LEU A 85 1 11
HELIX 6 6 HIS A 92 GLY A 100 1 9
HELIX 7 7 GLY A 100 SER A 107 1 8
HELIX 8 8 ASN A 115 ILE A 118 5 4
HELIX 9 9 LEU A 119 GLU A 124 1 6
HELIX 10 10 GLU A 124 GLY A 136 1 13
HELIX 11 11 SER A 171 LYS A 184 1 14
HELIX 12 12 THR A 189 ALA A 196 1 8
HELIX 13 13 ILE A 233 VAL A 237 1 5
HELIX 14 14 PRO A 240 GLU A 246 1 7
HELIX 15 15 ARG A 264 SER A 266 5 3
HELIX 16 16 LEU A 267 VAL A 286 1 20
HELIX 17 17 ASP A 316 MET A 323 5 8
HELIX 18 18 GLY A 326 TYR A 332 1 7
HELIX 19 19 SER A 338 ASP A 354 1 17
HELIX 20 20 MET A 355 LYS A 358 5 4
SHEET 1 A 4 LYS A 63 VAL A 67 0
SHEET 2 A 4 THR A 43 MET A 48 1 N CYS A 45 O LYS A 63
SHEET 3 A 4 THR A 20 LEU A 24 1 N ILE A 21 O VAL A 44
SHEET 4 A 4 SER A 87 VAL A 89 1 O ILE A 88 N ALA A 22
SHEET 1 B 2 MET A 112 PHE A 113 0
SHEET 2 B 2 ILE A 360 SER A 361 -1 O SER A 361 N MET A 112
SHEET 1 C 4 LYS A 142 TYR A 143 0
SHEET 2 C 4 HIS A 197 GLU A 200 -1 O ILE A 198 N TYR A 143
SHEET 3 C 4 VAL A 153 LYS A 156 -1 N LYS A 156 O HIS A 197
SHEET 4 C 4 PHE A 167 ALA A 169 -1 O ALA A 169 N VAL A 153
SHEET 1 D 5 TYR A 253 PRO A 260 0
SHEET 2 D 5 GLU A 219 ASN A 232 -1 N LYS A 227 O ILE A 259
SHEET 3 D 5 THR A 205 SER A 214 -1 N SER A 214 O GLU A 219
SHEET 4 D 5 GLY A 292 CYS A 300 -1 O PHE A 294 N TYR A 211
SHEET 5 D 5 LEU A 306 SER A 312 -1 O VAL A 307 N LEU A 299
CISPEP 1 SER A 231 ASN A 232 0 8.97
CISPEP 2 PRO A 287 PRO A 288 0 4.38
SITE 1 AC1 2 LYS A 56 ARG A 57
SITE 1 AC2 4 HIS A 210 PHE A 294 ASP A 316 THR A 319
SITE 1 AC3 15 ILE A 154 LYS A 156 TYR A 166 GLU A 199
SITE 2 AC3 15 GLU A 200 TYR A 201 GLU A 230 ARG A 238
SITE 3 AC3 15 TYR A 253 GLN A 297 LEU A 299 PHE A 309
SITE 4 AC3 15 GLU A 310 HOH A 606 HOH A 609
SITE 1 AC4 16 SER A 26 HIS A 27 SER A 94 ARG A 228
SITE 2 AC4 16 ILE A 255 ASN A 258 ARG A 264 SER A 266
SITE 3 AC4 16 ARG A 314 ASP A 316 GLY A 317 GLY A 318
SITE 4 AC4 16 HOH A 611 HOH A 612 HOH A 630 HOH A 660
CRYST1 108.001 108.001 254.275 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 0.009259 0.005346 0.000000 0.00000
SCALE2 0.000000 0.010692 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003933 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
