HEADER LYASE 24-MAY-07 2Q1C
TITLE 2-KETO-3-DEOXY-D-ARABINONATE DEHYDRATASE COMPLEXED WITH CALCIUM AND 2-
TITLE 2 OXOBUTYRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-KETO-3-DEOXY-D-ARABINONATE DEHYDRATASE;
COMPND 3 CHAIN: X;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 273057;
SOURCE 4 STRAIN: P2;
SOURCE 5 GENE: KDAD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET24-DERIVED
KEYWDS FAH-FAMILY FOLD, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.BARENDS,S.BROUNS,P.WORM,J.AKERBOOM,A.TURNBULL,L.SALMON
REVDAT 6 15-NOV-23 2Q1C 1 ATOM
REVDAT 5 30-AUG-23 2Q1C 1 REMARK
REVDAT 4 13-JUL-11 2Q1C 1 VERSN
REVDAT 3 24-FEB-09 2Q1C 1 VERSN
REVDAT 2 01-JUL-08 2Q1C 1 JRNL
REVDAT 1 08-APR-08 2Q1C 0
JRNL AUTH S.J.BROUNS,T.R.BARENDS,P.WORM,J.AKERBOOM,A.P.TURNBULL,
JRNL AUTH 2 L.SALMON,J.VAN DER OOST
JRNL TITL STRUCTURAL INSIGHT INTO SUBSTRATE BINDING AND CATALYSIS OF A
JRNL TITL 2 NOVEL 2-KETO-3-DEOXY-D-ARABINONATE DEHYDRATASE ILLUSTRATES
JRNL TITL 3 COMMON MECHANISTIC FEATURES OF THE FAH SUPERFAMILY.
JRNL REF J.MOL.BIOL. V. 379 357 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18448118
JRNL DOI 10.1016/J.JMB.2008.03.064
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 19.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 21834
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) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1156
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) : 1598
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2316
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.79000
REMARK 3 B22 (A**2) : 1.79000
REMARK 3 B33 (A**2) : -3.58000
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): 0.306
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.254
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.201
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.611
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
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): 2363 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3197 ; 1.028 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 290 ; 5.271 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;32.184 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 437 ;12.862 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;15.149 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 364 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1757 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1055 ; 0.166 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1628 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 106 ; 0.176 ; 1.000
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.099 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 43 ; 0.113 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.193 ; 1.000
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): 1515 ; 0.361 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2373 ; 0.648 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 974 ; 0.384 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 824 ; 0.672 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Q1C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043025.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, XFIT
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22992
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
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) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: XFIT
REMARK 200 STARTING MODEL: 1Q18
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA/K PHOSPHATE, PH 4.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 64.64500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 64.64500
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 111.54500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.64500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 55.77250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.64500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 167.31750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.64500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 167.31750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.64500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.77250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 64.64500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 64.64500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 111.54500
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 64.64500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 64.64500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 111.54500
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 64.64500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 167.31750
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 64.64500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 55.77250
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 64.64500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 55.77250
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 64.64500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 167.31750
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 64.64500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 64.64500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 111.54500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: THE BIOLOGICAL ASSEMBLY IS A TETRAMER. A TETRAMER CAN BE
REMARK 300 GENERATED WITH THE CRYSTALLOGRAPHIC SYMMETRY OPERATORS.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 ILE X 292
REMARK 465 THR X 293
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 X 21 -7.43 73.70
REMARK 500 PHE X 60 -59.73 132.61
REMARK 500 GLN X 61 77.34 87.96
REMARK 500 ASN X 63 -95.71 49.94
REMARK 500 THR X 68 -157.35 -151.07
REMARK 500 MET X 85 9.70 57.91
REMARK 500 ARG X 89 96.94 -56.11
REMARK 500 TYR X 90 82.41 61.99
REMARK 500 ASN X 174 127.12 -170.13
REMARK 500 ASP X 243 16.62 54.48
REMARK 500 ASN X 278 -15.99 73.43
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 CA X 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2KT X 295
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q18 RELATED DB: PDB
REMARK 900 RELATED ID: 2Q19 RELATED DB: PDB
REMARK 900 RELATED ID: 2Q1A RELATED DB: PDB
DBREF 2Q1C X 1 293 UNP Q97UA0 Q97UA0_SULSO 6 298
SEQRES 1 X 293 MET LYS LEU PHE ARG VAL VAL LYS ARG GLY TYR TYR ILE
SEQRES 2 X 293 SER TYR ALA ILE LEU ASP ASN SER THR ILE ILE ARG LEU
SEQRES 3 X 293 ASP GLU ASP PRO ILE LYS ALA LEU MET ARG TYR SER GLU
SEQRES 4 X 293 ASN LYS GLU VAL LEU GLY ASP ARG VAL THR GLY ILE ASP
SEQRES 5 X 293 TYR GLN SER LEU LEU LYS SER PHE GLN ILE ASN ASP ILE
SEQRES 6 X 293 ARG ILE THR LYS PRO ILE ASP PRO PRO GLU VAL TRP GLY
SEQRES 7 X 293 SER GLY ILE SER TYR GLU MET ALA ARG GLU ARG TYR SER
SEQRES 8 X 293 GLU GLU ASN VAL ALA LYS ILE LEU GLY LYS THR ILE TYR
SEQRES 9 X 293 GLU LYS VAL TYR ASP ALA VAL ARG PRO GLU ILE PHE PHE
SEQRES 10 X 293 LYS ALA THR PRO ASN ARG CYS VAL GLY HIS GLY GLU ALA
SEQRES 11 X 293 ILE ALA VAL ARG SER ASP SER GLU TRP THR LEU PRO GLU
SEQRES 12 X 293 PRO GLU LEU ALA VAL VAL LEU ASP SER ASN GLY LYS ILE
SEQRES 13 X 293 LEU GLY TYR THR ILE MET ASP ASP VAL SER ALA ARG ASP
SEQRES 14 X 293 LEU GLU ALA GLU ASN PRO LEU TYR LEU PRO GLN SER LYS
SEQRES 15 X 293 ILE TYR ALA GLY CYS CYS ALA PHE GLY PRO VAL ILE VAL
SEQRES 16 X 293 THR SER ASP GLU ILE LYS ASN PRO TYR SER LEU ASP ILE
SEQRES 17 X 293 THR LEU LYS ILE VAL ARG GLU GLY ARG VAL PHE PHE GLU
SEQRES 18 X 293 GLY SER VAL ASN THR ASN LYS MET ARG ARG LYS ILE GLU
SEQRES 19 X 293 GLU GLN ILE GLN TYR LEU ILE ARG ASP ASN PRO ILE PRO
SEQRES 20 X 293 ASP GLY THR ILE LEU THR THR GLY THR ALA ILE VAL PRO
SEQRES 21 X 293 GLY ARG ASP LYS GLY LEU LYS ASP GLU ASP ILE VAL GLU
SEQRES 22 X 293 ILE THR ILE SER ASN ILE GLY THR LEU ILE THR PRO VAL
SEQRES 23 X 293 LYS LYS ARG ARG LYS ILE THR
HET CA X 294 1
HET 2KT X 295 7
HETNAM CA CALCIUM ION
HETNAM 2KT 2-KETOBUTYRIC ACID
HETSYN 2KT 2-OXOBUTANOIC ACID
FORMUL 2 CA CA 2+
FORMUL 3 2KT C4 H6 O3
FORMUL 4 HOH *88(H2 O)
HELIX 1 1 ASP X 29 LYS X 41 1 13
HELIX 2 2 ASP X 52 SER X 59 1 8
HELIX 3 3 MET X 85 ARG X 89 5 5
HELIX 4 4 ILE X 103 ALA X 110 1 8
HELIX 5 5 THR X 120 ASN X 122 5 3
HELIX 6 6 ALA X 167 ASN X 174 1 8
HELIX 7 7 TYR X 177 ILE X 183 1 7
HELIX 8 8 ASP X 198 ILE X 200 5 3
HELIX 9 9 ASN X 227 MET X 229 5 3
HELIX 10 10 LYS X 232 ARG X 242 1 11
SHEET 1 A10 GLY X 45 ARG X 47 0
SHEET 2 A10 ILE X 23 LEU X 26 -1 N ARG X 25 O ASP X 46
SHEET 3 A10 TYR X 11 ILE X 17 -1 N ALA X 16 O ILE X 24
SHEET 4 A10 LYS X 2 LYS X 8 -1 N LYS X 8 O TYR X 11
SHEET 5 A10 CYS X 188 THR X 196 -1 O ILE X 194 N LEU X 3
SHEET 6 A10 ILE X 156 ASP X 164 -1 N ASP X 163 O ALA X 189
SHEET 7 A10 PRO X 144 LEU X 150 -1 N VAL X 149 O LEU X 157
SHEET 8 A10 THR X 250 THR X 253 -1 O THR X 250 N LEU X 150
SHEET 9 A10 VAL X 76 GLY X 80 1 N TRP X 77 O ILE X 251
SHEET 10 A10 GLU X 114 ALA X 119 -1 O PHE X 116 N GLY X 78
SHEET 1 B 5 GLN X 61 ILE X 62 0
SHEET 2 B 5 ILE X 65 ILE X 67 -1 O ILE X 65 N ILE X 62
SHEET 3 B 5 LYS X 2 LYS X 8 -1 N VAL X 7 O ARG X 66
SHEET 4 B 5 CYS X 188 THR X 196 -1 O ILE X 194 N LEU X 3
SHEET 5 B 5 CYS X 124 VAL X 125 1 N VAL X 125 O CYS X 188
SHEET 1 C 2 LYS X 97 ILE X 98 0
SHEET 2 C 2 LYS X 101 THR X 102 -1 O LYS X 101 N ILE X 98
SHEET 1 D 5 ILE X 131 VAL X 133 0
SHEET 2 D 5 GLY X 280 LYS X 288 1 O PRO X 285 N ILE X 131
SHEET 3 D 5 ILE X 271 ILE X 276 -1 N ILE X 274 O LEU X 282
SHEET 4 D 5 ASP X 207 ARG X 214 -1 N LYS X 211 O GLU X 273
SHEET 5 D 5 ARG X 217 ASN X 225 -1 O GLY X 222 N LEU X 210
CISPEP 1 PHE X 60 GLN X 61 0 2.40
CISPEP 2 GLU X 93 ASN X 94 0 -1.43
CISPEP 3 GLY X 191 PRO X 192 0 -5.10
SITE 1 AC1 5 GLU X 143 GLU X 145 ASP X 164 LYS X 182
SITE 2 AC1 5 HOH X 325
SITE 1 AC2 7 GLY X 80 ILE X 81 ARG X 89 GLU X 143
SITE 2 AC2 7 LYS X 182 GLY X 255 THR X 256
CRYST1 129.290 129.290 223.090 90.00 90.00 90.00 I 41 2 2 16
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 0.007735 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007735 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004482 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
