HEADER TRANSFERASE 18-JAN-12 4DD5
TITLE BIOSYNTHETIC THIOLASE (THLA1) FROM CLOSTRIDIUM DIFFICILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COA ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACETOACETYL-COA THIOLASE;
COMPND 5 EC: 2.3.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM DIFFICILE;
SOURCE 3 ORGANISM_TAXID: 272563;
SOURCE 4 STRAIN: 630;
SOURCE 5 GENE: CD630_10590, THLA, THLA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 2 DISEASES, CSGID, THIOLASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,Z.WAWRZAK,M.KUDRITSKA,A.EDWARDS,A.SAVCHENKO,
AUTHOR 2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 3 13-SEP-23 4DD5 1 SEQADV
REVDAT 2 15-NOV-17 4DD5 1 REMARK
REVDAT 1 01-FEB-12 4DD5 0
JRNL AUTH E.V.FILIPPOVA,Z.WAWRZAK,M.KUDRITSKA,A.EDWARDS,A.SAVCHENKO,
JRNL AUTH 2 W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL BIOSYNTHETIC THIOLASE (THLA1) FROM CLOSTRIDIUM DIFFICILE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 124443
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) : 0.118
REMARK 3 R VALUE (WORKING SET) : 0.117
REMARK 3 FREE R VALUE : 0.135
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6598
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) : 1.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8034
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 442
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2809
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 508
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.98000
REMARK 3 B22 (A**2) : -0.91000
REMARK 3 B33 (A**2) : -0.07000
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): 0.029
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.029
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.018
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.930
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.983
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.981
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3074 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2035 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4186 ; 1.563 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5042 ; 1.022 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 434 ; 6.345 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 112 ;37.598 ;25.536
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 554 ;11.970 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.463 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 489 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3581 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 563 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 3074 ; 4.002 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 20 ;19.708 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3210 ; 9.418 ; 5.000
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4DD5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : SI-111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131046
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.57000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 1DLV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M NH4 CITRATE, 0.1 M BIS-TRIS,
REMARK 280 PROPANE, PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 29.42500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.70550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 75.65450
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.42500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.70550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.65450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.42500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.70550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.65450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.42500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.70550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 75.65450
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 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 -1.000000 0.000000 0.000000 117.70000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 107.41100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 117.70000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 151.30900
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 107.41100
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 151.30900
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 MET A 1
REMARK 465 GLY A 2
REMARK 465 VAL A 3
REMARK 465 MET A 4
REMARK 465 ASN A 5
REMARK 465 GLY A 211
REMARK 465 ARG A 212
REMARK 465 LYS A 213
REMARK 465 GLY A 214
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 210 CD CE NZ
REMARK 470 LYS A 235 CE NZ
REMARK 470 ARG A 237 CD NE CZ NH1 NH2
REMARK 470 LYS A 242 CD CE NZ
REMARK 470 GLU A 306 CD OE1 OE2
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 ARG A 7 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 372 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 372 NE - CZ - NH2 ANGL. DEV. = 4.2 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 ASN A 69 80.42 47.34
REMARK 500 ASN A 69 81.23 47.34
REMARK 500 VAL A 92 -127.20 46.50
REMARK 500 ARG A 138 -57.11 73.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP05060 RELATED DB: TARGETTRACK
DBREF 4DD5 A 6 396 UNP Q18AR0 THLA_CLOD6 1 391
SEQADV 4DD5 MET A 1 UNP Q18AR0 EXPRESSION TAG
SEQADV 4DD5 GLY A 2 UNP Q18AR0 EXPRESSION TAG
SEQADV 4DD5 VAL A 3 UNP Q18AR0 EXPRESSION TAG
SEQADV 4DD5 MET A 4 UNP Q18AR0 EXPRESSION TAG
SEQADV 4DD5 ASN A 5 UNP Q18AR0 EXPRESSION TAG
SEQRES 1 A 396 MET GLY VAL MET ASN MET ARG GLU VAL VAL ILE ALA SER
SEQRES 2 A 396 ALA ALA ARG THR ALA VAL GLY SER PHE GLY GLY ALA PHE
SEQRES 3 A 396 LYS SER VAL SER ALA VAL GLU LEU GLY VAL THR ALA ALA
SEQRES 4 A 396 LYS GLU ALA ILE LYS ARG ALA ASN ILE THR PRO ASP MET
SEQRES 5 A 396 ILE ASP GLU SER LEU LEU GLY GLY VAL LEU THR ALA GLY
SEQRES 6 A 396 LEU GLY GLN ASN ILE ALA ARG GLN ILE ALA LEU GLY ALA
SEQRES 7 A 396 GLY ILE PRO VAL GLU LYS PRO ALA MET THR ILE ASN ILE
SEQRES 8 A 396 VAL CYS GLY SER GLY LEU ARG SER VAL SER MET ALA SER
SEQRES 9 A 396 GLN LEU ILE ALA LEU GLY ASP ALA ASP ILE MET LEU VAL
SEQRES 10 A 396 GLY GLY ALA GLU ASN MET SER MET SER PRO TYR LEU VAL
SEQRES 11 A 396 PRO SER ALA ARG TYR GLY ALA ARG MET GLY ASP ALA ALA
SEQRES 12 A 396 PHE VAL ASP SER MET ILE LYS ASP GLY LEU SER ASP ILE
SEQRES 13 A 396 PHE ASN ASN TYR HIS MET GLY ILE THR ALA GLU ASN ILE
SEQRES 14 A 396 ALA GLU GLN TRP ASN ILE THR ARG GLU GLU GLN ASP GLU
SEQRES 15 A 396 LEU ALA LEU ALA SER GLN ASN LYS ALA GLU LYS ALA GLN
SEQRES 16 A 396 ALA GLU GLY LYS PHE ASP GLU GLU ILE VAL PRO VAL VAL
SEQRES 17 A 396 ILE LYS GLY ARG LYS GLY ASP THR VAL VAL ASP LYS ASP
SEQRES 18 A 396 GLU TYR ILE LYS PRO GLY THR THR MET GLU LYS LEU ALA
SEQRES 19 A 396 LYS LEU ARG PRO ALA PHE LYS LYS ASP GLY THR VAL THR
SEQRES 20 A 396 ALA GLY ASN ALA SER GLY ILE ASN ASP GLY ALA ALA MET
SEQRES 21 A 396 LEU VAL VAL MET ALA LYS GLU LYS ALA GLU GLU LEU GLY
SEQRES 22 A 396 ILE GLU PRO LEU ALA THR ILE VAL SER TYR GLY THR ALA
SEQRES 23 A 396 GLY VAL ASP PRO LYS ILE MET GLY TYR GLY PRO VAL PRO
SEQRES 24 A 396 ALA THR LYS LYS ALA LEU GLU ALA ALA ASN MET THR ILE
SEQRES 25 A 396 GLU ASP ILE ASP LEU VAL GLU ALA ASN GLU ALA PHE ALA
SEQRES 26 A 396 ALA GLN SER VAL ALA VAL ILE ARG ASP LEU ASN ILE ASP
SEQRES 27 A 396 MET ASN LYS VAL ASN VAL ASN GLY GLY ALA ILE ALA ILE
SEQRES 28 A 396 GLY HIS PRO ILE GLY CYS SER GLY ALA ARG ILE LEU THR
SEQRES 29 A 396 THR LEU LEU TYR GLU MET LYS ARG ARG ASP ALA LYS THR
SEQRES 30 A 396 GLY LEU ALA THR LEU CYS ILE GLY GLY GLY MET GLY THR
SEQRES 31 A 396 THR LEU ILE VAL LYS ARG
FORMUL 2 HOH *508(H2 O)
HELIX 1 1 SER A 30 ALA A 46 1 17
HELIX 2 2 THR A 49 ILE A 53 5 5
HELIX 3 3 ASN A 69 ALA A 78 1 10
HELIX 4 4 ILE A 91 CYS A 93 5 3
HELIX 5 5 GLY A 94 LEU A 109 1 16
HELIX 6 6 SER A 147 GLY A 152 1 6
HELIX 7 7 MET A 162 ASN A 174 1 13
HELIX 8 8 THR A 176 GLU A 197 1 22
HELIX 9 9 THR A 229 LEU A 236 1 8
HELIX 10 10 LYS A 266 GLY A 273 1 8
HELIX 11 11 ASP A 289 TYR A 295 5 7
HELIX 12 12 GLY A 296 ASN A 309 1 14
HELIX 13 13 THR A 311 ILE A 315 5 5
HELIX 14 14 PHE A 324 ASN A 336 1 13
HELIX 15 15 GLY A 347 GLY A 352 1 6
HELIX 16 16 CYS A 357 ASP A 374 1 18
SHEET 1 A 5 GLY A 20 SER A 21 0
SHEET 2 A 5 ASN A 255 ALA A 265 -1 O ASP A 256 N GLY A 20
SHEET 3 A 5 ILE A 114 ASN A 122 -1 N MET A 115 O VAL A 263
SHEET 4 A 5 GLU A 55 GLY A 59 1 N GLY A 59 O GLY A 118
SHEET 5 A 5 ALA A 86 ILE A 89 1 O ILE A 89 N LEU A 58
SHEET 1 B 7 GLY A 20 SER A 21 0
SHEET 2 B 7 ASN A 255 ALA A 265 -1 O ASP A 256 N GLY A 20
SHEET 3 B 7 VAL A 9 ARG A 16 -1 N VAL A 10 O MET A 264
SHEET 4 B 7 ALA A 278 GLY A 287 -1 O ALA A 278 N ILE A 11
SHEET 5 B 7 MET A 388 LYS A 395 -1 O LYS A 395 N THR A 279
SHEET 6 B 7 THR A 377 ILE A 384 -1 N GLY A 378 O VAL A 394
SHEET 7 B 7 LEU A 317 ALA A 320 1 N GLU A 319 O LEU A 379
SHEET 1 C 2 TYR A 128 LEU A 129 0
SHEET 2 C 2 VAL A 145 ASP A 146 -1 O VAL A 145 N LEU A 129
SHEET 1 D 2 SER A 154 ASP A 155 0
SHEET 2 D 2 TYR A 160 HIS A 161 -1 O TYR A 160 N ASP A 155
SHEET 1 E 2 VAL A 207 ILE A 209 0
SHEET 2 E 2 THR A 216 VAL A 218 -1 O THR A 216 N ILE A 209
CRYST1 58.850 107.411 151.309 90.00 90.00 90.00 I 2 2 2 8
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 0.016992 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006609 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
