| content |
HEADER HYDROLASE 17-OCT-10 2XUA
TITLE CRYSTAL STRUCTURE OF THE ENOL-LACTONASE FROM BURKHOLDERIA
TITLE 2 XENOVORANS LB400
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-OXOADIPATE ENOL-LACTONASE;
COMPND 3 CHAIN: A, H;
COMPND 4 SYNONYM: PCAD;
COMPND 5 EC: 3.1.1.24
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;
SOURCE 3 ORGANISM_TAXID: 266265;
SOURCE 4 STRAIN: LB400;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET 28(A)
KEYWDS HYDROLASE, CATECHOL METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BAINS,L.KAUFMAN,B.FARNELL,M.J.BOULANGER
REVDAT 1 26-JAN-11 2XUA 0
JRNL AUTH J.BAINS,L.KAUFMAN,B.FARNELL,M.J.BOULANGER
JRNL TITL A PRODUCT ANALOG BOUND FORM OF 3-OXOADIPATE-ENOL- LACTONASE
JRNL TITL 2 (PCAD) REVEALS A MULTIFUNCTIONAL ROLE FOR THE DIVERGENT CAP
JRNL TITL 3 DOMAIN.
JRNL REF J.MOL.BIOL. 2011
JRNL REFN ESSN 1089-8638
JRNL PMID 21237173
JRNL DOI 10.1016/J.JMB.2011.01.007
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.77
REMARK 3 NUMBER OF REFLECTIONS : 34754
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) : 0.18542
REMARK 3 R VALUE (WORKING SET) : 0.18253
REMARK 3 FREE R VALUE : 0.24060
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1837
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) : 1.900
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.949
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2350
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.226
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.322
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3968
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 445
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.908
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02
REMARK 3 B22 (A**2) : 0.00
REMARK 3 B33 (A**2) : -0.02
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.713
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4061 ; 0.022 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5525 ; 1.984 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 519 ; 6.781 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 178 ;33.743 ;22.697
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 633 ;17.082 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;21.199 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 625 ; 0.162 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3114 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2589 ; 1.113 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4139 ; 1.871 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1472 ; 3.309 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1386 ; 5.004 ; 4.500
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2XUA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-10.
REMARK 100 THE PDBE ID CODE IS EBI-45795.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MX-325)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36592
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 36.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 6.9
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 33.36000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.58000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.36000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.58000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H
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 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 A2218 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 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MSE A 4
REMARK 465 GLN A 265
REMARK 465 LYS A 266
REMARK 465 GLY H 1
REMARK 465 SER H 2
REMARK 465 HIS H 3
REMARK 465 GLN H 265
REMARK 465 LYS H 266
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN A 10 O HOH A 2004 1.99
REMARK 500 CE MSE A 173 O HOH H 2039 2.00
REMARK 500 NH2 ARG H 166 O HOH H 2133 2.01
REMARK 500 OE1 GLU H 21 O HOH H 2019 2.04
REMARK 500 O VAL A 9 O HOH A 2003 2.12
REMARK 500 O HOH H 2038 O HOH H 2039 2.14
REMARK 500 OD1 ASP A 87 NH2 ARG A 116 2.16
REMARK 500 OE1 GLU A 264 O HOH A 2233 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 21 CB GLU A 21 CG -0.163
REMARK 500 GLU A 21 CG GLU A 21 CD -0.121
REMARK 500 TYR A 163 CD1 TYR A 163 CE1 0.093
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 39 CA - CB - CG ANGL. DEV. = 17.6 DEGREES
REMARK 500 LEU A 39 CB - CG - CD2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 LEU A 109 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG H 22 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 LEU H 39 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 LEU H 39 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG H 143 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG H 143 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG H 166 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG H 166 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 LEU H 171 CA - CB - CG ANGL. DEV. = -18.9 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 100 -112.82 54.62
REMARK 500 SER A 243 -135.34 -100.01
REMARK 500 ILE A 245 70.74 -100.80
REMARK 500 SER H 100 -116.46 55.23
REMARK 500 HIS H 113 48.04 -140.67
REMARK 500 SER H 243 -136.76 -94.24
REMARK 500 ILE H 245 67.15 -101.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 9 23.4 L L OUTSIDE RANGE
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 SHF H1265
DBREF 2XUA A 4 266 UNP Q13KT2 Q13KT2_BURXL 1 263
DBREF 2XUA H 4 266 UNP Q13KT2 Q13KT2_BURXL 1 263
SEQADV 2XUA GLY A 1 UNP Q13KT2 EXPRESSION TAG
SEQADV 2XUA SER A 2 UNP Q13KT2 EXPRESSION TAG
SEQADV 2XUA HIS A 3 UNP Q13KT2 EXPRESSION TAG
SEQADV 2XUA GLY H 1 UNP Q13KT2 EXPRESSION TAG
SEQADV 2XUA SER H 2 UNP Q13KT2 EXPRESSION TAG
SEQADV 2XUA HIS H 3 UNP Q13KT2 EXPRESSION TAG
SEQRES 1 A 266 GLY SER HIS MSE PRO TYR ALA ALA VAL ASN GLY THR GLU
SEQRES 2 A 266 LEU HIS TYR ARG ILE ASP GLY GLU ARG HIS GLY ASN ALA
SEQRES 3 A 266 PRO TRP ILE VAL LEU SER ASN SER LEU GLY THR ASP LEU
SEQRES 4 A 266 SER MSE TRP ALA PRO GLN VAL ALA ALA LEU SER LYS HIS
SEQRES 5 A 266 PHE ARG VAL LEU ARG TYR ASP THR ARG GLY HIS GLY HIS
SEQRES 6 A 266 SER GLU ALA PRO LYS GLY PRO TYR THR ILE GLU GLN LEU
SEQRES 7 A 266 THR GLY ASP VAL LEU GLY LEU MSE ASP THR LEU LYS ILE
SEQRES 8 A 266 ALA ARG ALA ASN PHE CYS GLY LEU SER MSE GLY GLY LEU
SEQRES 9 A 266 THR GLY VAL ALA LEU ALA ALA ARG HIS ALA ASP ARG ILE
SEQRES 10 A 266 GLU ARG VAL ALA LEU CYS ASN THR ALA ALA ARG ILE GLY
SEQRES 11 A 266 SER PRO GLU VAL TRP VAL PRO ARG ALA VAL LYS ALA ARG
SEQRES 12 A 266 THR GLU GLY MSE HIS ALA LEU ALA ASP ALA VAL LEU PRO
SEQRES 13 A 266 ARG TRP PHE THR ALA ASP TYR MSE GLU ARG GLU PRO VAL
SEQRES 14 A 266 VAL LEU ALA MSE ILE ARG ASP VAL PHE VAL HIS THR ASP
SEQRES 15 A 266 LYS GLU GLY TYR ALA SER ASN CYS GLU ALA ILE ASP ALA
SEQRES 16 A 266 ALA ASP LEU ARG PRO GLU ALA PRO GLY ILE LYS VAL PRO
SEQRES 17 A 266 ALA LEU VAL ILE SER GLY THR HIS ASP LEU ALA ALA THR
SEQRES 18 A 266 PRO ALA GLN GLY ARG GLU LEU ALA GLN ALA ILE ALA GLY
SEQRES 19 A 266 ALA ARG TYR VAL GLU LEU ASP ALA SER HIS ILE SER ASN
SEQRES 20 A 266 ILE GLU ARG ALA ASP ALA PHE THR LYS THR VAL VAL ASP
SEQRES 21 A 266 PHE LEU THR GLU GLN LYS
SEQRES 1 H 266 GLY SER HIS MSE PRO TYR ALA ALA VAL ASN GLY THR GLU
SEQRES 2 H 266 LEU HIS TYR ARG ILE ASP GLY GLU ARG HIS GLY ASN ALA
SEQRES 3 H 266 PRO TRP ILE VAL LEU SER ASN SER LEU GLY THR ASP LEU
SEQRES 4 H 266 SER MSE TRP ALA PRO GLN VAL ALA ALA LEU SER LYS HIS
SEQRES 5 H 266 PHE ARG VAL LEU ARG TYR ASP THR ARG GLY HIS GLY HIS
SEQRES 6 H 266 SER GLU ALA PRO LYS GLY PRO TYR THR ILE GLU GLN LEU
SEQRES 7 H 266 THR GLY ASP VAL LEU GLY LEU MSE ASP THR LEU LYS ILE
SEQRES 8 H 266 ALA ARG ALA ASN PHE CYS GLY LEU SER MSE GLY GLY LEU
SEQRES 9 H 266 THR GLY VAL ALA LEU ALA ALA ARG HIS ALA ASP ARG ILE
SEQRES 10 H 266 GLU ARG VAL ALA LEU CYS ASN THR ALA ALA ARG ILE GLY
SEQRES 11 H 266 SER PRO GLU VAL TRP VAL PRO ARG ALA VAL LYS ALA ARG
SEQRES 12 H 266 THR GLU GLY MSE HIS ALA LEU ALA ASP ALA VAL LEU PRO
SEQRES 13 H 266 ARG TRP PHE THR ALA ASP TYR MSE GLU ARG GLU PRO VAL
SEQRES 14 H 266 VAL LEU ALA MSE ILE ARG ASP VAL PHE VAL HIS THR ASP
SEQRES 15 H 266 LYS GLU GLY TYR ALA SER ASN CYS GLU ALA ILE ASP ALA
SEQRES 16 H 266 ALA ASP LEU ARG PRO GLU ALA PRO GLY ILE LYS VAL PRO
SEQRES 17 H 266 ALA LEU VAL ILE SER GLY THR HIS ASP LEU ALA ALA THR
SEQRES 18 H 266 PRO ALA GLN GLY ARG GLU LEU ALA GLN ALA ILE ALA GLY
SEQRES 19 H 266 ALA ARG TYR VAL GLU LEU ASP ALA SER HIS ILE SER ASN
SEQRES 20 H 266 ILE GLU ARG ALA ASP ALA PHE THR LYS THR VAL VAL ASP
SEQRES 21 H 266 PHE LEU THR GLU GLN LYS
MODRES 2XUA MSE A 41 MET SELENOMETHIONINE
MODRES 2XUA MSE A 86 MET SELENOMETHIONINE
MODRES 2XUA MSE A 101 MET SELENOMETHIONINE
MODRES 2XUA MSE A 147 MET SELENOMETHIONINE
MODRES 2XUA MSE A 164 MET SELENOMETHIONINE
MODRES 2XUA MSE A 173 MET SELENOMETHIONINE
MODRES 2XUA MSE H 4 MET SELENOMETHIONINE
MODRES 2XUA MSE H 41 MET SELENOMETHIONINE
MODRES 2XUA MSE H 86 MET SELENOMETHIONINE
MODRES 2XUA MSE H 101 MET SELENOMETHIONINE
MODRES 2XUA MSE H 147 MET SELENOMETHIONINE
MODRES 2XUA MSE H 164 MET SELENOMETHIONINE
MODRES 2XUA MSE H 173 MET SELENOMETHIONINE
HET MSE A 41 8
HET MSE A 86 8
HET MSE A 101 8
HET MSE A 147 8
HET MSE A 164 8
HET MSE A 173 8
HET MSE H 4 8
HET MSE H 41 8
HET MSE H 86 8
HET MSE H 101 8
HET MSE H 147 8
HET MSE H 164 8
HET MSE H 173 8
HET SHF H1265 8
HETNAM MSE SELENOMETHIONINE
HETNAM SHF LAEVULINIC ACID
FORMUL 3 MSE 13(C5 H11 N O2 SE)
FORMUL 4 SHF C5 H8 O3
FORMUL 5 HOH *445(H2 O)
HELIX 1 1 ASP A 38 PRO A 44 5 7
HELIX 2 2 GLN A 45 LYS A 51 1 7
HELIX 3 3 THR A 74 LEU A 89 1 16
HELIX 4 4 SER A 100 HIS A 113 1 14
HELIX 5 5 SER A 131 GLY A 146 1 16
HELIX 6 6 GLY A 146 PHE A 159 1 14
HELIX 7 7 THR A 160 GLU A 167 1 8
HELIX 8 8 GLU A 167 HIS A 180 1 14
HELIX 9 9 ASP A 182 ALA A 196 1 15
HELIX 10 10 LEU A 198 ILE A 205 5 8
HELIX 11 11 THR A 221 ILE A 232 1 12
HELIX 12 12 ILE A 245 ARG A 250 1 6
HELIX 13 13 ARG A 250 THR A 263 1 14
HELIX 14 14 ASP H 38 MSE H 41 5 4
HELIX 15 15 TRP H 42 PHE H 53 1 12
HELIX 16 16 THR H 74 LEU H 89 1 16
HELIX 17 17 SER H 100 HIS H 113 1 14
HELIX 18 18 SER H 131 GLY H 146 1 16
HELIX 19 19 GLY H 146 LEU H 155 1 10
HELIX 20 20 PRO H 156 TRP H 158 5 3
HELIX 21 21 THR H 160 GLU H 167 1 8
HELIX 22 22 GLU H 167 HIS H 180 1 14
HELIX 23 23 ASP H 182 ALA H 196 1 15
HELIX 24 24 GLU H 201 ILE H 205 5 5
HELIX 25 25 THR H 221 ILE H 232 1 12
HELIX 26 26 ILE H 245 ARG H 250 1 6
HELIX 27 27 ARG H 250 GLU H 264 1 15
SHEET 1 AA 8 TYR A 6 ALA A 8 0
SHEET 2 AA 8 GLU A 13 ASP A 19 -1 O LEU A 14 N ALA A 7
SHEET 3 AA 8 ARG A 54 TYR A 58 -1 O VAL A 55 N ASP A 19
SHEET 4 AA 8 TRP A 28 SER A 32 1 O ILE A 29 N LEU A 56
SHEET 5 AA 8 ALA A 94 LEU A 99 1 O ASN A 95 N VAL A 30
SHEET 6 AA 8 ILE A 117 CYS A 123 1 N GLU A 118 O ALA A 94
SHEET 7 AA 8 ALA A 209 GLY A 214 1 O LEU A 210 N LEU A 122
SHEET 8 AA 8 ARG A 236 LEU A 240 1 O ARG A 236 N VAL A 211
SHEET 1 HA 8 TYR H 6 VAL H 9 0
SHEET 2 HA 8 THR H 12 ASP H 19 -1 O THR H 12 N VAL H 9
SHEET 3 HA 8 ARG H 54 TYR H 58 -1 O VAL H 55 N ASP H 19
SHEET 4 HA 8 TRP H 28 SER H 32 1 O ILE H 29 N LEU H 56
SHEET 5 HA 8 ALA H 94 LEU H 99 1 O ASN H 95 N VAL H 30
SHEET 6 HA 8 ILE H 117 CYS H 123 1 N GLU H 118 O ALA H 94
SHEET 7 HA 8 ALA H 209 GLY H 214 1 O LEU H 210 N LEU H 122
SHEET 8 HA 8 ARG H 236 LEU H 240 1 O ARG H 236 N VAL H 211
LINK C SER A 40 N MSE A 41 1555 1555 1.33
LINK C MSE A 41 N TRP A 42 1555 1555 1.34
LINK C LEU A 85 N MSE A 86 1555 1555 1.33
LINK C MSE A 86 N ASP A 87 1555 1555 1.35
LINK C SER A 100 N MSE A 101 1555 1555 1.34
LINK C MSE A 101 N GLY A 102 1555 1555 1.33
LINK C GLY A 146 N MSE A 147 1555 1555 1.33
LINK C MSE A 147 N HIS A 148 1555 1555 1.34
LINK C TYR A 163 N MSE A 164 1555 1555 1.32
LINK C MSE A 164 N GLU A 165 1555 1555 1.33
LINK C ALA A 172 N MSE A 173 1555 1555 1.34
LINK C MSE A 173 N ILE A 174 1555 1555 1.33
LINK C MSE H 4 N PRO H 5 1555 1555 1.36
LINK C SER H 40 N MSE H 41 1555 1555 1.34
LINK C MSE H 41 N TRP H 42 1555 1555 1.35
LINK C LEU H 85 N MSE H 86 1555 1555 1.34
LINK C MSE H 86 N ASP H 87 1555 1555 1.33
LINK C SER H 100 N MSE H 101 1555 1555 1.34
LINK C MSE H 101 N GLY H 102 1555 1555 1.34
LINK C GLY H 146 N MSE H 147 1555 1555 1.33
LINK C MSE H 147 N HIS H 148 1555 1555 1.33
LINK C TYR H 163 N MSE H 164 1555 1555 1.34
LINK C MSE H 164 N GLU H 165 1555 1555 1.32
LINK C ALA H 172 N MSE H 173 1555 1555 1.33
LINK C MSE H 173 N ILE H 174 1555 1555 1.33
CISPEP 1 GLY A 71 PRO A 72 0 -1.18
CISPEP 2 GLY H 71 PRO H 72 0 7.46
SITE 1 AC1 11 SER H 34 LEU H 35 ARG H 138 VAL H 154
SITE 2 AC1 11 ARG H 157 TRP H 158 PHE H 178 TYR H 186
SITE 3 AC1 11 ALA H 219 HOH H2015 HOH H2194
CRYST1 66.720 101.160 72.520 90.00 90.00 90.00 P 21 21 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 0.014988 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013789 0.00000
TER 1981 GLU A 264
TER 3970 GLU H 264
MASTER 374 0 14 27 16 0 3 6 4421 2 137 42
END |