HEADER UNKNOWN FUNCTION 13-JAN-15 4XLL
TITLE TOXOPLASMA GONDII DJ-1, OXIDIZED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DJ-1 FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;
SOURCE 3 ORGANISM_TAXID: 5811;
SOURCE 4 GENE: TGVEG_214290;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15
KEYWDS OXIDIZED, DJ-1, PSEUDOPROTEASE, PAPAIN-FOLD, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.CHILD,M.A.WILSON,M.L.REESE,M.BOGYO
REVDAT 2 27-JUL-16 4XLL 1 REMARK
REVDAT 1 11-FEB-15 4XLL 0
JRNL AUTH M.A.CHILD,M.GARLAND,P.MADZELAN,M.TREECK,W.VAN DER LINDEN,
JRNL AUTH 2 K.ORESIC,E.WEERAPANA,M.A.WILSON,J.C.BOOTHROYD,M.L.REESE,
JRNL AUTH 3 M.BOGYO
JRNL TITL TOXOPLASMA DJ-1 REGULATES MICRONEME EXOCYTOSIS THROUGH AN
JRNL TITL 2 ASSOCIATION WITH THE PLANT-LIKE KINASE, CDPK1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 18630
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1811
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 REFLECTION IN BIN (WORKING SET) : 993
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2742
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.60000
REMARK 3 B22 (A**2) : -2.93000
REMARK 3 B33 (A**2) : -1.84000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.35000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.316
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.208
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.686
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2780 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2791 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3765 ; 1.668 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6433 ; 1.032 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 368 ; 6.636 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;34.919 ;24.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 495 ;13.265 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;12.574 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 459 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3105 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 547 ; 0.004 ; 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): 1472 ; 1.269 ; 1.761
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1471 ; 1.264 ; 1.759
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1837 ; 2.003 ; 2.632
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): 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 185 B 2 185 11647 0.080 0.050
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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2264 10.3196 11.2328
REMARK 3 T TENSOR
REMARK 3 T11: 0.0094 T22: 0.0479
REMARK 3 T33: 0.0302 T12: -0.0012
REMARK 3 T13: -0.0060 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.0180 L22: 0.1916
REMARK 3 L33: 0.2286 L12: -0.0001
REMARK 3 L13: 0.0038 L23: -0.0437
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: -0.0073 S13: -0.0015
REMARK 3 S21: -0.0309 S22: 0.0076 S23: 0.0095
REMARK 3 S31: 0.0268 S32: -0.0017 S33: -0.0023
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 185
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8749 32.3746 26.4324
REMARK 3 T TENSOR
REMARK 3 T11: 0.0101 T22: 0.0485
REMARK 3 T33: 0.0352 T12: 0.0047
REMARK 3 T13: -0.0101 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.1536 L22: 0.1292
REMARK 3 L33: 0.2310 L12: 0.0439
REMARK 3 L13: -0.0494 L23: 0.0773
REMARK 3 S TENSOR
REMARK 3 S11: -0.0137 S12: -0.0176 S13: -0.0050
REMARK 3 S21: -0.0102 S22: 0.0132 S23: 0.0103
REMARK 3 S31: -0.0261 S32: 0.0078 S33: 0.0004
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 4XLL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205903.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979450
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JULY 4, 2012
REMARK 200 DATA SCALING SOFTWARE : XSCALE VERSION JULY 4, 2012
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18638
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 38.693
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 6.840
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.250
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 5MG/ML PROTEIN IN 10 MM HEPES 7.0,
REMARK 280 100 MM NACL, 10 MM DTT MIXED WITH RESERVOIR: 1.5 M AMMONIUM
REMARK 280 CITRATE TRIBASIC, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 27.59050
REMARK 290 SMTRY3 2 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: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
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 SG CYS A 127 O HOH A 238 1.84
REMARK 500 O HOH B 241 O HOH B 247 2.08
REMARK 500 O HOH A 240 O HOH A 247 2.10
REMARK 500 O HOH B 222 O HOH B 278 2.16
REMARK 500 OE1 GLU B 159 O HOH B 316 2.17
REMARK 500 O HOH B 225 O HOH B 227 2.17
REMARK 500 O ARG B 26 O HOH B 201 2.19
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 CSD A 104 -118.78 73.97
REMARK 500 ASN A 146 -113.02 52.15
REMARK 500 TYR A 169 -101.95 -113.71
REMARK 500 LEU A 182 33.53 74.22
REMARK 500 CSD B 104 -120.30 72.86
REMARK 500 ASN B 146 -113.58 52.04
REMARK 500 TYR B 169 -101.89 -115.71
REMARK 500 LEU B 182 34.61 72.86
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4XLL A 1 185 UNP B9PZH8 B9PZH8_TOXGO 72 256
DBREF 4XLL B 1 185 UNP B9PZH8 B9PZH8_TOXGO 72 256
SEQADV 4XLL GLY A -2 UNP B9PZH8 EXPRESSION TAG
SEQADV 4XLL SER A -1 UNP B9PZH8 EXPRESSION TAG
SEQADV 4XLL HIS A 0 UNP B9PZH8 EXPRESSION TAG
SEQADV 4XLL GLY B -2 UNP B9PZH8 EXPRESSION TAG
SEQADV 4XLL SER B -1 UNP B9PZH8 EXPRESSION TAG
SEQADV 4XLL HIS B 0 UNP B9PZH8 EXPRESSION TAG
SEQRES 1 A 188 GLY SER HIS MET ALA VAL LYS VAL LEU VAL PRO VAL ALA
SEQRES 2 A 188 HIS ASP SER GLU GLU ILE GLU ALA VAL SER ILE ILE ASP
SEQRES 3 A 188 THR LEU ARG ARG ALA GLY ALA GLU VAL VAL VAL ALA SER
SEQRES 4 A 188 VAL GLU ASP THR GLU ILE VAL ARG MET SER ARG GLY VAL
SEQRES 5 A 188 CYS VAL LYS ALA ASP LYS LEU ILE SER ALA VAL GLU ASN
SEQRES 6 A 188 GLU THR TYR ASP CYS ILE ALA ILE PRO GLY GLY MET PRO
SEQRES 7 A 188 GLY ALA GLU ARG CYS ARG ASP SER ALA ALA LEU THR ALA
SEQRES 8 A 188 MET LEU LYS THR HIS LYS ALA GLN GLY LYS LEU ILE ALA
SEQRES 9 A 188 ALA ILE CSD ALA SER PRO ALA VAL VAL LEU GLN THR HIS
SEQRES 10 A 188 GLY LEU LEU GLN GLY GLU LYS ALA VAL ALA TYR PRO CYS
SEQRES 11 A 188 PHE MET ASP GLN PHE PRO ALA ASP MET ARG GLY GLU GLY
SEQRES 12 A 188 ARG VAL CYS VAL SER ASN LYS ILE VAL THR SER VAL GLY
SEQRES 13 A 188 PRO SER SER ALA ILE GLU PHE ALA LEU LYS LEU ILE GLU
SEQRES 14 A 188 VAL LEU TYR ASN LYS GLU GLN ALA LYS LYS ILE ALA ALA
SEQRES 15 A 188 GLN LEU LEU TYR ALA TYR
SEQRES 1 B 188 GLY SER HIS MET ALA VAL LYS VAL LEU VAL PRO VAL ALA
SEQRES 2 B 188 HIS ASP SER GLU GLU ILE GLU ALA VAL SER ILE ILE ASP
SEQRES 3 B 188 THR LEU ARG ARG ALA GLY ALA GLU VAL VAL VAL ALA SER
SEQRES 4 B 188 VAL GLU ASP THR GLU ILE VAL ARG MET SER ARG GLY VAL
SEQRES 5 B 188 CYS VAL LYS ALA ASP LYS LEU ILE SER ALA VAL GLU ASN
SEQRES 6 B 188 GLU THR TYR ASP CYS ILE ALA ILE PRO GLY GLY MET PRO
SEQRES 7 B 188 GLY ALA GLU ARG CYS ARG ASP SER ALA ALA LEU THR ALA
SEQRES 8 B 188 MET LEU LYS THR HIS LYS ALA GLN GLY LYS LEU ILE ALA
SEQRES 9 B 188 ALA ILE CSD ALA SER PRO ALA VAL VAL LEU GLN THR HIS
SEQRES 10 B 188 GLY LEU LEU GLN GLY GLU LYS ALA VAL ALA TYR PRO CYS
SEQRES 11 B 188 PHE MET ASP GLN PHE PRO ALA ASP MET ARG GLY GLU GLY
SEQRES 12 B 188 ARG VAL CYS VAL SER ASN LYS ILE VAL THR SER VAL GLY
SEQRES 13 B 188 PRO SER SER ALA ILE GLU PHE ALA LEU LYS LEU ILE GLU
SEQRES 14 B 188 VAL LEU TYR ASN LYS GLU GLN ALA LYS LYS ILE ALA ALA
SEQRES 15 B 188 GLN LEU LEU TYR ALA TYR
MODRES 4XLL CSD A 104 CYS MODIFIED RESIDUE
MODRES 4XLL CSD B 104 CYS MODIFIED RESIDUE
HET CSD A 104 8
HET CSD B 104 8
HETNAM CSD 3-SULFINOALANINE
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 3 HOH *245(H2 O)
HELIX 1 AA1 GLU A 14 ALA A 28 1 15
HELIX 2 AA2 SER A 58 GLU A 61 5 4
HELIX 3 AA3 PRO A 75 SER A 83 1 9
HELIX 4 AA4 SER A 83 GLN A 96 1 14
HELIX 5 AA5 ALA A 105 VAL A 110 1 6
HELIX 6 AA6 TYR A 125 PHE A 132 5 8
HELIX 7 AA7 PRO A 133 ARG A 137 5 5
HELIX 8 AA8 GLY A 153 SER A 155 5 3
HELIX 9 AA9 SER A 156 TYR A 169 1 14
HELIX 10 AB1 ASN A 170 LEU A 182 1 13
HELIX 11 AB2 GLU B 14 ALA B 28 1 15
HELIX 12 AB3 SER B 58 GLU B 61 5 4
HELIX 13 AB4 PRO B 75 ASP B 82 1 8
HELIX 14 AB5 SER B 83 GLN B 96 1 14
HELIX 15 AB6 ALA B 105 VAL B 110 1 6
HELIX 16 AB7 TYR B 125 PHE B 132 5 8
HELIX 17 AB8 PRO B 133 ARG B 137 5 5
HELIX 18 AB9 GLY B 153 SER B 155 5 3
HELIX 19 AC1 SER B 156 TYR B 169 1 14
HELIX 20 AC2 ASN B 170 LEU B 182 1 13
SHEET 1 AA1 7 LYS A 55 LEU A 56 0
SHEET 2 AA1 7 GLU A 31 SER A 36 1 N SER A 36 O LYS A 55
SHEET 3 AA1 7 LYS A 4 VAL A 9 1 N VAL A 5 O GLU A 31
SHEET 4 AA1 7 CYS A 67 ILE A 70 1 O ALA A 69 N LEU A 6
SHEET 5 AA1 7 LEU A 99 ILE A 103 1 O ALA A 101 N ILE A 68
SHEET 6 AA1 7 ILE A 148 SER A 151 1 O VAL A 149 N ALA A 102
SHEET 7 AA1 7 VAL A 142 SER A 145 -1 N SER A 145 O ILE A 148
SHEET 1 AA2 4 ILE A 42 ARG A 44 0
SHEET 2 AA2 4 CYS A 50 LYS A 52 -1 O VAL A 51 N VAL A 43
SHEET 3 AA2 4 CYS B 50 LYS B 52 -1 O CYS B 50 N LYS A 52
SHEET 4 AA2 4 ILE B 42 ARG B 44 -1 N VAL B 43 O VAL B 51
SHEET 1 AA3 7 LYS B 55 LEU B 56 0
SHEET 2 AA3 7 GLU B 31 SER B 36 1 N SER B 36 O LYS B 55
SHEET 3 AA3 7 LYS B 4 VAL B 9 1 N VAL B 5 O GLU B 31
SHEET 4 AA3 7 CYS B 67 ILE B 70 1 O ALA B 69 N LEU B 6
SHEET 5 AA3 7 LEU B 99 ILE B 103 1 O ALA B 101 N ILE B 70
SHEET 6 AA3 7 ILE B 148 SER B 151 1 O VAL B 149 N ALA B 102
SHEET 7 AA3 7 VAL B 142 SER B 145 -1 N SER B 145 O ILE B 148
LINK C ILE A 103 N CSD A 104 1555 1555 1.34
LINK C CSD A 104 N ALA A 105 1555 1555 1.33
LINK C ILE B 103 N CSD B 104 1555 1555 1.34
LINK C CSD B 104 N ALA B 105 1555 1555 1.34
CISPEP 1 MET A 74 PRO A 75 0 2.23
CISPEP 2 MET B 74 PRO B 75 0 2.65
CRYST1 38.777 55.181 75.247 90.00 93.92 90.00 P 1 21 1 4
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 0.025788 0.000000 0.001767 0.00000
SCALE2 0.000000 0.018122 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013321 0.00000
(ATOM LINES ARE NOT SHOWN.)
END