HEADER LYASE 22-JUL-13 4LSB
TITLE CRYSTAL STRUCTURE OF A PUTATIVE LYASE/MUTASE FROM BURKHOLDERIA
TITLE 2 CENOCEPACIA J2315
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYASE/MUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA;
SOURCE 3 ORGANISM_TAXID: 216591;
SOURCE 4 STRAIN: J2315;
SOURCE 5 GENE: BCEJ2315_55920, BCAM2155;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 3 INFECTIOUS DISEASE, SSGCID, LYASE, MUTASE, CYSTIC FIBROSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 20-SEP-23 4LSB 1 REMARK SEQADV LINK
REVDAT 1 14-AUG-13 4LSB 0
JRNL AUTH SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 2 (SSGCID)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE LYASE/MUTASE FROM
JRNL TITL 2 BURKHOLDERIA CENOCEPACIA J2315
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 45828
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2440
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3243
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3986
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 402
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.16000
REMARK 3 B22 (A**2) : -1.39000
REMARK 3 B33 (A**2) : -1.77000
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): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.690
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4058 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3825 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5537 ; 1.568 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8710 ; 0.852 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 552 ; 5.708 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 170 ;37.325 ;22.706
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 546 ;12.392 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;15.041 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 640 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4792 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 928 ; 0.001 ; 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): 2217 ; 1.338 ; 1.706
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2216 ; 1.334 ; 1.705
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2766 ; 2.064 ; 2.548
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2767 ; 2.065 ; 2.550
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1841 ; 1.881 ; 1.910
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1841 ; 1.878 ; 1.909
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2771 ; 2.882 ; 2.788
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4906 ; 4.951 ;14.956
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4703 ; 4.769 ;14.395
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 281
REMARK 3 RESIDUE RANGE : A 501 A 501
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4829 -16.3837 18.5583
REMARK 3 T TENSOR
REMARK 3 T11: 0.0421 T22: 0.0322
REMARK 3 T33: 0.0147 T12: -0.0052
REMARK 3 T13: -0.0125 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.0201 L22: 0.2523
REMARK 3 L33: 0.7267 L12: -0.0495
REMARK 3 L13: 0.0543 L23: 0.0956
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: -0.0053 S13: 0.0001
REMARK 3 S21: -0.0433 S22: -0.0346 S23: 0.0055
REMARK 3 S31: 0.0025 S32: -0.0477 S33: 0.0225
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 282
REMARK 3 RESIDUE RANGE : B 501 B 501
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5896 -15.7474 52.2718
REMARK 3 T TENSOR
REMARK 3 T11: 0.0570 T22: 0.0170
REMARK 3 T33: 0.0351 T12: 0.0001
REMARK 3 T13: 0.0007 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.2381 L22: 0.1374
REMARK 3 L33: 0.5392 L12: -0.1708
REMARK 3 L13: 0.1295 L23: -0.1135
REMARK 3 S TENSOR
REMARK 3 S11: -0.0344 S12: 0.0228 S13: -0.0693
REMARK 3 S21: 0.0407 S22: 0.0010 S23: 0.0504
REMARK 3 S31: -0.0266 S32: 0.0113 S33: 0.0334
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 4LSB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000081023.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48518
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.97
REMARK 200 R MERGE FOR SHELL (I) : 0.46600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2ZE3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.2M MGCL2, TRIS HCL PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.53000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.93000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.01500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.93000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.53000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.01500
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: 5440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 -7
REMARK 465 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 ARG A 3
REMARK 465 SER A 4
REMARK 465 ILE A 282
REMARK 465 LEU A 283
REMARK 465 PHE A 284
REMARK 465 ASP A 285
REMARK 465 GLU A 286
REMARK 465 MET B -7
REMARK 465 ALA B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 ARG B 3
REMARK 465 ALA B 63
REMARK 465 LEU B 283
REMARK 465 PHE B 284
REMARK 465 ASP B 285
REMARK 465 GLU B 286
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 5 CG OD1 OD2
REMARK 470 ARG A 15 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 62 CG OD1 ND2
REMARK 470 ILE A 64 CG1 CG2 CD1
REMARK 470 ARG A 145 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 268 CG CD NE CZ NH1 NH2
REMARK 470 SER A 280 OG
REMARK 470 PRO A 281 CG CD
REMARK 470 SER B 4 OG
REMARK 470 ASP B 5 CG OD1 OD2
REMARK 470 ARG B 9 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 62 CG OD1 ND2
REMARK 470 ILE B 64 CG1 CG2 CD1
REMARK 470 ASP B 124 CG OD1 OD2
REMARK 470 ARG B 164 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 213 CG CD1 CD2
REMARK 470 GLN B 214 CG CD OE1 NE2
REMARK 470 ARG B 254 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 282 CG1 CG2 CD1
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 101 CD GLU A 101 OE1 0.085
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 ARG A 201 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PRO A 281 C - N - CA ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG B 145 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 145 NE - CZ - NH2 ANGL. DEV. = -3.2 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 GLU A 89 -136.42 50.36
REMARK 500 GLU B 89 -131.39 48.20
REMARK 500 GLN B 214 -150.61 -138.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 4 ASP B 5 139.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 50 OG
REMARK 620 2 HOH A 713 O 78.4
REMARK 620 3 HOH A 714 O 68.4 91.7
REMARK 620 4 HOH A 715 O 111.0 157.5 110.7
REMARK 620 5 HOH A 716 O 104.0 96.9 167.2 61.4
REMARK 620 6 HOH A 802 O 150.3 77.2 95.6 98.0 95.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 50 OG
REMARK 620 2 GLU B 89 OE2 90.6
REMARK 620 3 HOH B 746 O 90.4 83.0
REMARK 620 4 HOH B 747 O 176.6 89.6 86.3
REMARK 620 5 HOH B 781 O 82.0 168.3 88.0 97.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZE3 RELATED DB: PDB
REMARK 900 RELATED ID: 3FA3 RELATED DB: PDB
REMARK 900 RELATED ID: SSGCID-BUCEA.00014.A RELATED DB: TARGETTRACK
DBREF 4LSB A 1 286 UNP B4EFV2 B4EFV2_BURCJ 1 286
DBREF 4LSB B 1 286 UNP B4EFV2 B4EFV2_BURCJ 1 286
SEQADV 4LSB MET A -7 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB ALA A -6 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS A -5 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS A -4 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS A -3 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS A -2 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS A -1 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS A 0 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB MET B -7 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB ALA B -6 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS B -5 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS B -4 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS B -3 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS B -2 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS B -1 UNP B4EFV2 EXPRESSION TAG
SEQADV 4LSB HIS B 0 UNP B4EFV2 EXPRESSION TAG
SEQRES 1 A 294 MET ALA HIS HIS HIS HIS HIS HIS MET ILE ARG SER ASP
SEQRES 2 A 294 LEU GLN ALA ARG HIS ALA GLU ALA PHE ARG ALA LEU HIS
SEQRES 3 A 294 THR ARG PRO GLY ALA PHE ILE ILE PRO ASN PRO TRP ASP
SEQRES 4 A 294 ALA GLY THR ALA ARG LEU LEU ALA MET ALA GLY PHE GLU
SEQRES 5 A 294 ALA LEU ALA THR THR SER ALA GLY TYR ALA PHE SER LYS
SEQRES 6 A 294 GLY GLN PRO ASP ASN ALA ILE ASP ARG ASP ALA MET LEU
SEQRES 7 A 294 ASP HIS ILE ALA ASP LEU VAL ALA ALA GLY GLY LEU PRO
SEQRES 8 A 294 VAL SER ALA ASP LEU GLU ASN GLY PHE GLY ASP ALA PRO
SEQRES 9 A 294 GLY THR VAL ALA GLU THR ILE ARG LEU ALA ALA GLU ALA
SEQRES 10 A 294 GLY ALA VAL GLY GLY SER ILE GLU ASP ALA THR GLY ARG
SEQRES 11 A 294 ALA ASP THR PRO ILE TYR ALA ARG ASP ALA SER VAL GLU
SEQRES 12 A 294 ARG ILE ALA ALA ALA VAL ASP ALA ALA ARG ALA LEU PRO
SEQRES 13 A 294 PHE PRO PHE THR LEU THR ALA ARG CYS GLU ASN TYR LEU
SEQRES 14 A 294 HIS GLY ARG ARG ASP LEU ASP ASP THR ILE ALA ARG LEU
SEQRES 15 A 294 VAL ALA TYR ARG ASP ALA GLY ALA ASP VAL LEU TYR ALA
SEQRES 16 A 294 PRO GLY ILE THR ASP ALA ASP GLU ILE ALA ALA VAL THR
SEQRES 17 A 294 ARG ALA VAL GLY ALA PRO VAL ASN VAL VAL MET GLY LEU
SEQRES 18 A 294 GLN GLY GLY LEU LEU SER LEU ASP GLU LEU ALA ALA LEU
SEQRES 19 A 294 GLY VAL LYS ARG VAL SER VAL GLY GLY ALA LEU ALA ARG
SEQRES 20 A 294 ALA ALA LEU GLY ALA PHE LEU ARG ALA ALA THR GLU MET
SEQRES 21 A 294 ARG ARG ASP GLY THR PHE THR PHE THR GLN ALA ALA VAL
SEQRES 22 A 294 PRO GLY ARG ASP ILE ASN ARG TRP PHE ALA ALA PRO ASP
SEQRES 23 A 294 ASN SER PRO ILE LEU PHE ASP GLU
SEQRES 1 B 294 MET ALA HIS HIS HIS HIS HIS HIS MET ILE ARG SER ASP
SEQRES 2 B 294 LEU GLN ALA ARG HIS ALA GLU ALA PHE ARG ALA LEU HIS
SEQRES 3 B 294 THR ARG PRO GLY ALA PHE ILE ILE PRO ASN PRO TRP ASP
SEQRES 4 B 294 ALA GLY THR ALA ARG LEU LEU ALA MET ALA GLY PHE GLU
SEQRES 5 B 294 ALA LEU ALA THR THR SER ALA GLY TYR ALA PHE SER LYS
SEQRES 6 B 294 GLY GLN PRO ASP ASN ALA ILE ASP ARG ASP ALA MET LEU
SEQRES 7 B 294 ASP HIS ILE ALA ASP LEU VAL ALA ALA GLY GLY LEU PRO
SEQRES 8 B 294 VAL SER ALA ASP LEU GLU ASN GLY PHE GLY ASP ALA PRO
SEQRES 9 B 294 GLY THR VAL ALA GLU THR ILE ARG LEU ALA ALA GLU ALA
SEQRES 10 B 294 GLY ALA VAL GLY GLY SER ILE GLU ASP ALA THR GLY ARG
SEQRES 11 B 294 ALA ASP THR PRO ILE TYR ALA ARG ASP ALA SER VAL GLU
SEQRES 12 B 294 ARG ILE ALA ALA ALA VAL ASP ALA ALA ARG ALA LEU PRO
SEQRES 13 B 294 PHE PRO PHE THR LEU THR ALA ARG CYS GLU ASN TYR LEU
SEQRES 14 B 294 HIS GLY ARG ARG ASP LEU ASP ASP THR ILE ALA ARG LEU
SEQRES 15 B 294 VAL ALA TYR ARG ASP ALA GLY ALA ASP VAL LEU TYR ALA
SEQRES 16 B 294 PRO GLY ILE THR ASP ALA ASP GLU ILE ALA ALA VAL THR
SEQRES 17 B 294 ARG ALA VAL GLY ALA PRO VAL ASN VAL VAL MET GLY LEU
SEQRES 18 B 294 GLN GLY GLY LEU LEU SER LEU ASP GLU LEU ALA ALA LEU
SEQRES 19 B 294 GLY VAL LYS ARG VAL SER VAL GLY GLY ALA LEU ALA ARG
SEQRES 20 B 294 ALA ALA LEU GLY ALA PHE LEU ARG ALA ALA THR GLU MET
SEQRES 21 B 294 ARG ARG ASP GLY THR PHE THR PHE THR GLN ALA ALA VAL
SEQRES 22 B 294 PRO GLY ARG ASP ILE ASN ARG TRP PHE ALA ALA PRO ASP
SEQRES 23 B 294 ASN SER PRO ILE LEU PHE ASP GLU
HET MG A 501 1
HET CL A 502 1
HET MG B 501 1
HET CL B 502 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 MG 2(MG 2+)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *402(H2 O)
HELIX 1 1 ASP A 5 ARG A 20 1 16
HELIX 2 2 ASP A 31 ALA A 41 1 11
HELIX 3 3 THR A 49 LYS A 57 1 9
HELIX 4 4 ASP A 65 GLY A 81 1 17
HELIX 5 5 ALA A 95 ALA A 109 1 15
HELIX 6 6 ALA A 129 LEU A 147 1 19
HELIX 7 7 GLU A 158 HIS A 162 5 5
HELIX 8 8 ASP A 166 GLY A 181 1 16
HELIX 9 9 ASP A 192 GLY A 204 1 13
HELIX 10 10 SER A 219 LEU A 226 1 8
HELIX 11 11 GLY A 235 GLY A 256 1 22
HELIX 12 12 PHE A 258 ALA A 264 5 7
HELIX 13 13 PRO A 266 ALA A 276 1 11
HELIX 14 14 ASP B 5 HIS B 18 1 14
HELIX 15 15 ASP B 31 ALA B 41 1 11
HELIX 16 16 THR B 49 LYS B 57 1 9
HELIX 17 17 ASP B 65 GLY B 81 1 17
HELIX 18 18 ALA B 95 ALA B 109 1 15
HELIX 19 19 ALA B 129 ALA B 146 1 18
HELIX 20 20 GLU B 158 HIS B 162 5 5
HELIX 21 21 ASP B 166 ALA B 180 1 15
HELIX 22 22 ASP B 192 GLY B 204 1 13
HELIX 23 23 SER B 219 LEU B 226 1 8
HELIX 24 24 GLY B 235 GLY B 256 1 22
HELIX 25 25 PHE B 258 ALA B 264 5 7
HELIX 26 26 PRO B 266 ALA B 276 1 11
SHEET 1 A 8 PHE A 24 ILE A 26 0
SHEET 2 A 8 ARG A 230 SER A 232 1 O VAL A 231 N ILE A 26
SHEET 3 A 8 VAL A 207 VAL A 210 1 N VAL A 209 O ARG A 230
SHEET 4 A 8 VAL A 184 TYR A 186 1 N LEU A 185 O ASN A 208
SHEET 5 A 8 THR A 152 ARG A 156 1 N ALA A 155 O VAL A 184
SHEET 6 A 8 GLY A 113 GLU A 117 1 N GLY A 114 O THR A 154
SHEET 7 A 8 VAL A 84 ASP A 87 1 N ALA A 86 O GLY A 113
SHEET 8 A 8 LEU A 46 ALA A 47 1 N LEU A 46 O SER A 85
SHEET 1 B 8 PHE B 24 ILE B 26 0
SHEET 2 B 8 ARG B 230 SER B 232 1 O VAL B 231 N ILE B 26
SHEET 3 B 8 VAL B 207 VAL B 210 1 N VAL B 209 O ARG B 230
SHEET 4 B 8 VAL B 184 TYR B 186 1 N LEU B 185 O ASN B 208
SHEET 5 B 8 THR B 152 ARG B 156 1 N ALA B 155 O VAL B 184
SHEET 6 B 8 GLY B 113 GLU B 117 1 N GLY B 114 O THR B 154
SHEET 7 B 8 VAL B 84 ASP B 87 1 N ALA B 86 O GLY B 113
SHEET 8 B 8 LEU B 46 ALA B 47 1 N LEU B 46 O SER B 85
LINK OG SER A 50 MG MG A 501 1555 1555 2.50
LINK MG MG A 501 O HOH A 713 1555 1555 2.29
LINK MG MG A 501 O HOH A 714 1555 1555 1.75
LINK MG MG A 501 O HOH A 715 1555 1555 1.90
LINK MG MG A 501 O HOH A 716 1555 1555 2.93
LINK MG MG A 501 O HOH A 802 1555 1555 2.15
LINK OG SER B 50 MG MG B 501 1555 1555 2.41
LINK OE2 GLU B 89 MG MG B 501 1555 1555 2.08
LINK MG MG B 501 O HOH B 746 1555 1555 2.42
LINK MG MG B 501 O HOH B 747 1555 1555 2.18
LINK MG MG B 501 O HOH B 781 1555 1555 2.03
SITE 1 AC1 7 SER A 50 ASP A 61 HOH A 713 HOH A 714
SITE 2 AC1 7 HOH A 715 HOH A 716 HOH A 802
SITE 1 AC2 3 ALA A 51 ARG A 239 HOH A 606
SITE 1 AC3 6 SER B 50 ASP B 61 GLU B 89 HOH B 746
SITE 2 AC3 6 HOH B 747 HOH B 781
SITE 1 AC4 2 GLY B 235 ARG B 239
CRYST1 53.060 70.030 141.860 90.00 90.00 90.00 P 21 21 21 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 0.018847 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007049 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
