HEADER MOLYBDENUM COFACTOR BIOSYNTHESIS 28-NOV-02 1O8N
TITLE THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSYNTHETIC PROTEIN DOMAIN
TITLE 2 CNX1G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOLYBDOPTERIN BIOSYNTHESIS CNX1 PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CNX1 G-DOMAIN, RESIDUES 462-628;
COMPND 5 SYNONYM: MOLYBDENUM COFACTOR, BIOSYNTHESIS ENZYME CNX1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 STRAIN: CV. COLUMBIA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: RK5206;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PQE60
KEYWDS MOLYBDENUM COFACTOR BIOSYNTHESIS, CNX1G, MUTANTS
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KUPER,J.WINKING,H.J.HECHT,G.SCHWARZ,R.R.MENDEL
REVDAT 3 13-DEC-23 1O8N 1 REMARK
REVDAT 2 24-FEB-09 1O8N 1 VERSN
REVDAT 1 27-FEB-03 1O8N 0
JRNL AUTH J.KUPER,J.WINKING,H.J.HECHT,R.R.MENDEL,G.SCHWARZ
JRNL TITL THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSYNTHETIC
JRNL TITL 2 PROTEIN DOMAIN CNX1G
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 411 36 2003
JRNL REFN ISSN 0003-9861
JRNL PMID 12590921
JRNL DOI 10.1016/S0003-9861(02)00714-2
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 15773
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 844
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1128
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3582
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : 0.89000
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): 0.945
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.317
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.221
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.964
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3633 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3516 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4923 ; 1.488 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8211 ; 0.846 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 483 ; 5.001 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 597 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3978 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 612 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 765 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3940 ; 0.249 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2140 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 93 ; 0.173 ; 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): 5 ; 0.157 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 27 ; 0.332 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.206 ; 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): 2421 ; 0.801 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3912 ; 1.575 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1212 ; 2.181 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1011 ; 4.171 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 4 A 28 4
REMARK 3 1 B 4 B 28 4
REMARK 3 1 C 4 C 28 4
REMARK 3 2 A 30 A 44 4
REMARK 3 2 B 30 B 44 4
REMARK 3 2 C 30 C 44 4
REMARK 3 3 A 46 A 162 4
REMARK 3 3 B 46 B 162 4
REMARK 3 3 C 46 C 162 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2290 ; 0.17 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2290 ; 0.17 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2290 ; 0.22 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2290 ; 0.40 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2290 ; 0.47 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2290 ; 0.46 ; 2.00
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 : 1.40
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 1O8N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1290011743.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : OSMIX MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU IMAGE PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15774
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 87.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.15700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1EAV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM ACETATE 0.1 M SODIUM
REMARK 280 CACODYLATE, PH 6.5, PH 6.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 61.24300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 61.24300
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.18000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 61.24300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.59000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 61.24300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 130.77000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 61.24300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 130.77000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.24300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 43.59000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 61.24300
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 61.24300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 87.18000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 61.24300
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 61.24300
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 87.18000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 61.24300
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 130.77000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 61.24300
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 43.59000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 61.24300
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 43.59000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 61.24300
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 130.77000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 61.24300
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 61.24300
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 87.18000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION IN CHAIN A, THR 542 ALA
REMARK 400 ENGINEERED MUTATION IN CHAIN B, THR 542 ALA
REMARK 400 ENGINEERED MUTATION IN CHAIN C, THR 542 ALA
REMARK 400
REMARK 400 THE MOLECULE CNX1G IS INVOLVED IN MOLYBDENUM COFACTOR
REMARK 400 BIOSYNTHESIS
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 VAL A 1
REMARK 465 PRO A 2
REMARK 465 LYS A 166
REMARK 465 ARG A 167
REMARK 465 VAL B 1
REMARK 465 PRO B 2
REMARK 465 LYS B 166
REMARK 465 ARG B 167
REMARK 465 VAL C 1
REMARK 465 PRO C 2
REMARK 465 LYS C 166
REMARK 465 ARG C 167
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 ASP A 165 CA C O CB CG OD1 OD2
REMARK 470 ASP B 165 CA C O CB CG OD1 OD2
REMARK 470 ASP C 165 CA C O CB CG OD1 OD2
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 87 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 70 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP C 24 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP C 70 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP C 73 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP C 87 CB - CG - OD2 ANGL. DEV. = 6.4 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 SER A 14 115.94 -174.30
REMARK 500 SER B 14 113.15 -177.31
REMARK 500 ASP B 87 97.92 -65.35
REMARK 500 PRO C 4 142.04 -39.51
REMARK 500 SER C 14 107.71 175.98
REMARK 500 ASP C 87 102.23 -56.73
REMARK 500 THR C 116 143.72 -172.74
REMARK 500 SER C 124 134.45 -35.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EAV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF HUMAN GEPHYRIN AND PLANT CNX1 G DOMAINS -
REMARK 900 COMPARATIVE ANALYSIS AND FUNCTIONAL IMPLICATIONS
REMARK 900 RELATED ID: 1O8O RELATED DB: PDB
REMARK 900 THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSENTHETIC PROTEIN
REMARK 900 DOMAIN CNX1G
REMARK 900 RELATED ID: 1O8Q RELATED DB: PDB
REMARK 900 THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSENTHETIC PROTEIN
REMARK 900 DOMAIN CNX1G
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DOMAIN DEFINITION MODIFIED FROM SWALL:CNX1_ARATH_2
REMARK 999 N-TERMINAL EXTENSION VPGP,
REMARK 999 C-TERMINAL EXTENSION KQIKGDK
DBREF 1O8N A 1 167 UNP Q39054 CNX1_ARATH 462 628
DBREF 1O8N B 1 167 UNP Q39054 CNX1_ARATH 462 628
DBREF 1O8N C 1 167 UNP Q39054 CNX1_ARATH 462 628
SEQADV 1O8N ALA A 81 UNP Q39054 THR 542 ENGINEERED MUTATION
SEQADV 1O8N ALA B 81 UNP Q39054 THR 542 ENGINEERED MUTATION
SEQADV 1O8N ALA C 81 UNP Q39054 THR 542 ENGINEERED MUTATION
SEQRES 1 A 167 VAL PRO GLY PRO GLU TYR LYS VAL ALA ILE LEU THR VAL
SEQRES 2 A 167 SER ASP THR VAL SER ALA GLY ALA GLY PRO ASP ARG SER
SEQRES 3 A 167 GLY PRO ARG ALA VAL SER VAL VAL ASP SER SER SER GLU
SEQRES 4 A 167 LYS LEU GLY GLY ALA LYS VAL VAL ALA THR ALA VAL VAL
SEQRES 5 A 167 PRO ASP GLU VAL GLU ARG ILE LYS ASP ILE LEU GLN LYS
SEQRES 6 A 167 TRP SER ASP VAL ASP GLU MET ASP LEU ILE LEU THR LEU
SEQRES 7 A 167 GLY GLY ALA GLY PHE THR PRO ARG ASP VAL THR PRO GLU
SEQRES 8 A 167 ALA THR LYS LYS VAL ILE GLU ARG GLU THR PRO GLY LEU
SEQRES 9 A 167 LEU PHE VAL MET MET GLN GLU SER LEU LYS ILE THR PRO
SEQRES 10 A 167 PHE ALA MET LEU SER ARG SER ALA ALA GLY ILE ARG GLY
SEQRES 11 A 167 SER THR LEU ILE ILE ASN MET PRO GLY ASN PRO ASN ALA
SEQRES 12 A 167 VAL ALA GLU CYS MET GLU ALA LEU LEU PRO ALA LEU LYS
SEQRES 13 A 167 HIS ALA LEU LYS GLN ILE LYS GLY ASP LYS ARG
SEQRES 1 B 167 VAL PRO GLY PRO GLU TYR LYS VAL ALA ILE LEU THR VAL
SEQRES 2 B 167 SER ASP THR VAL SER ALA GLY ALA GLY PRO ASP ARG SER
SEQRES 3 B 167 GLY PRO ARG ALA VAL SER VAL VAL ASP SER SER SER GLU
SEQRES 4 B 167 LYS LEU GLY GLY ALA LYS VAL VAL ALA THR ALA VAL VAL
SEQRES 5 B 167 PRO ASP GLU VAL GLU ARG ILE LYS ASP ILE LEU GLN LYS
SEQRES 6 B 167 TRP SER ASP VAL ASP GLU MET ASP LEU ILE LEU THR LEU
SEQRES 7 B 167 GLY GLY ALA GLY PHE THR PRO ARG ASP VAL THR PRO GLU
SEQRES 8 B 167 ALA THR LYS LYS VAL ILE GLU ARG GLU THR PRO GLY LEU
SEQRES 9 B 167 LEU PHE VAL MET MET GLN GLU SER LEU LYS ILE THR PRO
SEQRES 10 B 167 PHE ALA MET LEU SER ARG SER ALA ALA GLY ILE ARG GLY
SEQRES 11 B 167 SER THR LEU ILE ILE ASN MET PRO GLY ASN PRO ASN ALA
SEQRES 12 B 167 VAL ALA GLU CYS MET GLU ALA LEU LEU PRO ALA LEU LYS
SEQRES 13 B 167 HIS ALA LEU LYS GLN ILE LYS GLY ASP LYS ARG
SEQRES 1 C 167 VAL PRO GLY PRO GLU TYR LYS VAL ALA ILE LEU THR VAL
SEQRES 2 C 167 SER ASP THR VAL SER ALA GLY ALA GLY PRO ASP ARG SER
SEQRES 3 C 167 GLY PRO ARG ALA VAL SER VAL VAL ASP SER SER SER GLU
SEQRES 4 C 167 LYS LEU GLY GLY ALA LYS VAL VAL ALA THR ALA VAL VAL
SEQRES 5 C 167 PRO ASP GLU VAL GLU ARG ILE LYS ASP ILE LEU GLN LYS
SEQRES 6 C 167 TRP SER ASP VAL ASP GLU MET ASP LEU ILE LEU THR LEU
SEQRES 7 C 167 GLY GLY ALA GLY PHE THR PRO ARG ASP VAL THR PRO GLU
SEQRES 8 C 167 ALA THR LYS LYS VAL ILE GLU ARG GLU THR PRO GLY LEU
SEQRES 9 C 167 LEU PHE VAL MET MET GLN GLU SER LEU LYS ILE THR PRO
SEQRES 10 C 167 PHE ALA MET LEU SER ARG SER ALA ALA GLY ILE ARG GLY
SEQRES 11 C 167 SER THR LEU ILE ILE ASN MET PRO GLY ASN PRO ASN ALA
SEQRES 12 C 167 VAL ALA GLU CYS MET GLU ALA LEU LEU PRO ALA LEU LYS
SEQRES 13 C 167 HIS ALA LEU LYS GLN ILE LYS GLY ASP LYS ARG
FORMUL 4 HOH *49(H2 O)
HELIX 1 1 SER A 14 ALA A 19 1 6
HELIX 2 2 ARG A 25 SER A 37 1 13
HELIX 3 3 GLU A 55 VAL A 69 1 15
HELIX 4 4 VAL A 88 ILE A 97 1 10
HELIX 5 5 THR A 101 THR A 116 1 16
HELIX 6 6 PRO A 117 SER A 122 5 6
HELIX 7 7 ASN A 140 GLY A 164 1 25
HELIX 8 8 SER B 14 ALA B 19 1 6
HELIX 9 9 SER B 26 SER B 37 1 12
HELIX 10 10 GLU B 55 VAL B 69 1 15
HELIX 11 11 VAL B 88 ILE B 97 1 10
HELIX 12 12 THR B 101 THR B 116 1 16
HELIX 13 13 PRO B 117 SER B 122 5 6
HELIX 14 14 ASN B 140 GLY B 164 1 25
HELIX 15 15 SER C 14 ALA C 19 1 6
HELIX 16 16 ARG C 25 SER C 38 1 14
HELIX 17 17 GLU C 55 VAL C 69 1 15
HELIX 18 18 VAL C 88 ILE C 97 1 10
HELIX 19 19 THR C 101 LYS C 114 1 14
HELIX 20 20 THR C 116 SER C 122 5 7
HELIX 21 21 ASN C 140 GLY C 164 1 25
SHEET 1 AA 6 ALA A 44 VAL A 52 0
SHEET 2 AA 6 TYR A 6 VAL A 13 1 O TYR A 6 N LYS A 45
SHEET 3 AA 6 LEU A 74 LEU A 78 1 O LEU A 74 N ALA A 9
SHEET 4 AA 6 THR A 132 MET A 137 1 O LEU A 133 N ILE A 75
SHEET 5 AA 6 ALA A 126 ARG A 129 -1 O GLY A 127 N ILE A 134
SHEET 6 AA 6 ARG A 99 GLU A 100 -1 O ARG A 99 N ILE A 128
SHEET 1 BA 6 ALA B 44 VAL B 52 0
SHEET 2 BA 6 TYR B 6 VAL B 13 1 O TYR B 6 N LYS B 45
SHEET 3 BA 6 LEU B 74 LEU B 78 1 O LEU B 74 N ALA B 9
SHEET 4 BA 6 THR B 132 MET B 137 1 O LEU B 133 N ILE B 75
SHEET 5 BA 6 ALA B 126 ARG B 129 -1 O GLY B 127 N ILE B 134
SHEET 6 BA 6 ARG B 99 GLU B 100 -1 O ARG B 99 N ILE B 128
SHEET 1 CA 6 ALA C 44 VAL C 52 0
SHEET 2 CA 6 TYR C 6 VAL C 13 1 O TYR C 6 N LYS C 45
SHEET 3 CA 6 LEU C 74 LEU C 78 1 O LEU C 74 N ALA C 9
SHEET 4 CA 6 THR C 132 MET C 137 1 O LEU C 133 N ILE C 75
SHEET 5 CA 6 ALA C 126 ARG C 129 -1 O GLY C 127 N ILE C 134
SHEET 6 CA 6 ARG C 99 GLU C 100 -1 O ARG C 99 N ILE C 128
CRYST1 122.486 122.486 174.360 90.00 90.00 90.00 I 41 2 2 48
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 0.008164 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005735 0.00000
MTRIX1 1 0.491908 0.630518 0.600395 53.60710 1
MTRIX2 1 -0.360731 -0.480023 0.799657 44.82480 1
MTRIX3 1 0.792401 -0.609939 -0.008679 -84.97820 1
MTRIX1 2 0.496506 -0.378581 0.781126 -3.61500 1
MTRIX2 2 0.621857 -0.472707 -0.624373 110.09260 1
MTRIX3 2 0.605619 0.795754 0.000722 -14.45150 1
(ATOM LINES ARE NOT SHOWN.)
END