HEADER TRANSFERASE 10-FEB-05 1YT8
TITLE CRYSTAL STRUCTURE OF THIOSULFATE SULFURTRANSFERASE FROM PSEUDOMONAS
TITLE 2 AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOSULFATE SULFURTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.8.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOSULFATE SULFURTRANSFERASE, RHODANASE DOMAINS, CYANIDE
KEYWDS 2 DETOXIFICATION, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 4 NYSGXRC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KUMARAN,S.SWAMINATHAN,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 4 03-FEB-21 1YT8 1 AUTHOR REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1YT8 1 VERSN
REVDAT 2 06-MAY-08 1YT8 1 COMPND VERSN
REVDAT 1 22-MAR-05 1YT8 0
JRNL AUTH D.KUMARAN,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF THIOSULFATE SULFURTRANSFERASE FROM
JRNL TITL 2 PSEUDOMONAS AERUGINOSA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 470811.160
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 55493
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 SET) : 0.185
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1667
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8589
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 240
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4030
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 524
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.80000
REMARK 3 B22 (A**2) : 6.38000
REMARK 3 B33 (A**2) : -2.58000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.10
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 32.24
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031904.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979, 0.976, 0.94
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CBASS
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56427
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 98.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULFATE, SODIUM
REMARK 280 CACODYLATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295K
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 44.17400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.23800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.17400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.23800
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: MONOMERIC
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 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 MSE A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 GLN A 5
REMARK 465 GLY A 531
REMARK 465 GLY A 532
REMARK 465 SER A 533
REMARK 465 HIS A 534
REMARK 465 HIS A 535
REMARK 465 HIS A 536
REMARK 465 HIS A 537
REMARK 465 HIS A 538
REMARK 465 HIS A 539
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 193 S SO3 A 540 2.00
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 ALA A 38 126.27 -174.21
REMARK 500 ASP A 111 -167.72 72.24
REMARK 500 VAL A 333 -56.41 -122.73
REMARK 500 ARG A 407 134.52 -172.26
REMARK 500 CYS A 437 -172.30 -171.86
REMARK 500 SER A 440 -3.72 93.55
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 SO3 A 540
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 541
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T1653 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE ELECTRON DENSITY FOR THE SIDE CHAIN OF RESIDUE 84
REMARK 999 SUPPORTS A HIS RATHER THAN A LEU AND MODELED ACCORDINGLY.
DBREF 1YT8 A 4 529 UNP Q9I0N4 Q9I0N4_PSEAE 2 527
SEQADV 1YT8 MSE A 1 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 SER A 2 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 LEU A 3 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 HIS A 84 UNP Q9I0N4 LEU 82 SEE REMARK 999
SEQADV 1YT8 MSE A 161 UNP Q9I0N4 MET 159 MODIFIED RESIDUE
SEQADV 1YT8 MSE A 337 UNP Q9I0N4 MET 335 MODIFIED RESIDUE
SEQADV 1YT8 MSE A 345 UNP Q9I0N4 MET 343 MODIFIED RESIDUE
SEQADV 1YT8 MSE A 504 UNP Q9I0N4 MET 502 MODIFIED RESIDUE
SEQADV 1YT8 GLU A 530 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 GLY A 531 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 GLY A 532 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 SER A 533 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 HIS A 534 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 HIS A 535 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 HIS A 536 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 HIS A 537 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 HIS A 538 UNP Q9I0N4 EXPRESSION TAG
SEQADV 1YT8 HIS A 539 UNP Q9I0N4 EXPRESSION TAG
SEQRES 1 A 539 MSE SER LEU SER GLN ILE ALA VAL ARG THR PHE HIS ASP
SEQRES 2 A 539 ILE ARG ALA ALA LEU LEU ALA ARG ARG GLU LEU ALA LEU
SEQRES 3 A 539 LEU ASP VAL ARG GLU GLU ASP PRO PHE ALA GLN ALA HIS
SEQRES 4 A 539 PRO LEU PHE ALA ALA ASN LEU PRO LEU SER ARG LEU GLU
SEQRES 5 A 539 LEU GLU ILE HIS ALA ARG VAL PRO ARG ARG ASP THR PRO
SEQRES 6 A 539 ILE THR VAL TYR ASP ASP GLY GLU GLY LEU ALA PRO VAL
SEQRES 7 A 539 ALA ALA GLN ARG LEU HIS ASP LEU GLY TYR SER ASP VAL
SEQRES 8 A 539 ALA LEU LEU ASP GLY GLY LEU SER GLY TRP ARG ASN ALA
SEQRES 9 A 539 GLY GLY GLU LEU PHE ARG ASP VAL ASN VAL PRO SER LYS
SEQRES 10 A 539 ALA PHE GLY GLU LEU VAL GLU ALA GLU ARG HIS THR PRO
SEQRES 11 A 539 SER LEU ALA ALA GLU GLU VAL GLN ALA LEU LEU ASP ALA
SEQRES 12 A 539 ARG ALA GLU ALA VAL ILE LEU ASP ALA ARG ARG PHE ASP
SEQRES 13 A 539 GLU TYR GLN THR MSE SER ILE PRO GLY GLY ILE SER VAL
SEQRES 14 A 539 PRO GLY ALA GLU LEU VAL LEU ARG VAL ALA GLU LEU ALA
SEQRES 15 A 539 PRO ASP PRO ARG THR ARG VAL ILE VAL ASN CYS ALA GLY
SEQRES 16 A 539 ARG THR ARG SER ILE ILE GLY THR GLN SER LEU LEU ASN
SEQRES 17 A 539 ALA GLY ILE PRO ASN PRO VAL ALA ALA LEU ARG ASN GLY
SEQRES 18 A 539 THR ILE GLY TRP THR LEU ALA GLY GLN GLN LEU GLU HIS
SEQRES 19 A 539 GLY GLN THR ARG ARG PHE GLY ALA ILE SER GLN ASP THR
SEQRES 20 A 539 ARG LYS ALA ALA ALA GLN ARG ALA ARG ALA VAL ALA ASP
SEQRES 21 A 539 ARG ALA GLY VAL GLU ARG LEU ASP LEU ALA GLY LEU ALA
SEQRES 22 A 539 GLN TRP GLN ASP GLU HIS ASP ARG THR THR TYR LEU LEU
SEQRES 23 A 539 ASP VAL ARG THR PRO GLU GLU TYR GLU ALA GLY HIS LEU
SEQRES 24 A 539 PRO GLY SER ARG SER THR PRO GLY GLY GLN LEU VAL GLN
SEQRES 25 A 539 GLU THR ASP HIS VAL ALA SER VAL ARG GLY ALA ARG LEU
SEQRES 26 A 539 VAL LEU VAL ASP ASP ASP GLY VAL ARG ALA ASN MSE SER
SEQRES 27 A 539 ALA SER TRP LEU ALA GLN MSE GLY TRP GLN VAL ALA VAL
SEQRES 28 A 539 LEU ASP GLY LEU SER GLU ALA ASP PHE SER GLU ARG GLY
SEQRES 29 A 539 ALA TRP SER ALA PRO LEU PRO ARG GLN PRO ARG ALA ASP
SEQRES 30 A 539 THR ILE ASP PRO THR THR LEU ALA ASP TRP LEU GLY GLU
SEQRES 31 A 539 PRO GLY THR ARG VAL LEU ASP PHE THR ALA SER ALA ASN
SEQRES 32 A 539 TYR ALA LYS ARG HIS ILE PRO GLY ALA ALA TRP VAL LEU
SEQRES 33 A 539 ARG SER GLN LEU LYS GLN ALA LEU GLU ARG LEU GLY THR
SEQRES 34 A 539 ALA GLU ARG TYR VAL LEU THR CYS GLY SER SER LEU LEU
SEQRES 35 A 539 ALA ARG PHE ALA VAL ALA GLU VAL GLN ALA LEU SER GLY
SEQRES 36 A 539 LYS PRO VAL PHE LEU LEU ASP GLY GLY THR SER ALA TRP
SEQRES 37 A 539 VAL ALA ALA GLY LEU PRO THR GLU ASP GLY GLU SER LEU
SEQRES 38 A 539 LEU ALA SER PRO ARG ILE ASP ARG TYR ARG ARG PRO TYR
SEQRES 39 A 539 GLU GLY THR ASP ASN PRO ARG GLU ALA MSE GLN GLY TYR
SEQRES 40 A 539 LEU ASP TRP GLU PHE GLY LEU VAL GLU GLN LEU GLY ARG
SEQRES 41 A 539 ASP GLY THR HIS GLY PHE PHE VAL ILE GLU GLY GLY SER
SEQRES 42 A 539 HIS HIS HIS HIS HIS HIS
MODRES 1YT8 MSE A 161 MET SELENOMETHIONINE
MODRES 1YT8 MSE A 337 MET SELENOMETHIONINE
MODRES 1YT8 MSE A 345 MET SELENOMETHIONINE
MODRES 1YT8 MSE A 504 MET SELENOMETHIONINE
HET MSE A 161 8
HET MSE A 337 8
HET MSE A 345 8
HET MSE A 504 8
HET SO3 A 540 4
HET GOL A 541 6
HETNAM MSE SELENOMETHIONINE
HETNAM SO3 SULFITE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 SO3 O3 S 2-
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *524(H2 O)
HELIX 1 1 THR A 10 ARG A 21 1 12
HELIX 2 2 GLU A 31 ALA A 36 1 6
HELIX 3 3 PRO A 47 SER A 49 5 3
HELIX 4 4 ARG A 50 VAL A 59 1 10
HELIX 5 5 GLY A 74 LEU A 86 1 13
HELIX 6 6 GLY A 96 ALA A 104 1 9
HELIX 7 7 ASN A 113 HIS A 128 1 16
HELIX 8 8 ALA A 133 ALA A 143 1 11
HELIX 9 9 ARG A 154 MSE A 161 1 8
HELIX 10 10 PRO A 170 ALA A 172 5 3
HELIX 11 11 GLU A 173 ALA A 182 1 10
HELIX 12 12 ARG A 196 ALA A 209 1 14
HELIX 13 13 ASN A 220 ALA A 228 1 9
HELIX 14 14 SER A 244 GLY A 263 1 20
HELIX 15 15 ASP A 268 GLU A 278 1 11
HELIX 16 16 THR A 290 GLY A 297 1 8
HELIX 17 17 PRO A 306 GLU A 313 1 8
HELIX 18 18 GLU A 313 ALA A 318 1 6
HELIX 19 19 VAL A 333 MSE A 345 1 13
HELIX 20 20 SER A 356 PHE A 360 5 5
HELIX 21 21 ASP A 380 LEU A 388 1 9
HELIX 22 22 ALA A 400 ARG A 407 1 8
HELIX 23 23 LEU A 416 SER A 418 5 3
HELIX 24 24 GLN A 419 GLY A 428 1 10
HELIX 25 25 SER A 440 GLY A 455 1 16
HELIX 26 26 GLY A 463 ALA A 471 1 9
HELIX 27 27 PRO A 500 GLY A 513 1 14
HELIX 28 28 GLY A 513 GLY A 522 1 10
SHEET 1 A 5 ALA A 7 ARG A 9 0
SHEET 2 A 5 VAL A 91 LEU A 94 1 O LEU A 93 N ARG A 9
SHEET 3 A 5 ILE A 66 TYR A 69 1 N VAL A 68 O ALA A 92
SHEET 4 A 5 ALA A 25 ASP A 28 1 N ALA A 25 O THR A 67
SHEET 5 A 5 ALA A 44 ASN A 45 1 O ALA A 44 N LEU A 26
SHEET 1 B 5 SER A 131 LEU A 132 0
SHEET 2 B 5 VAL A 215 LEU A 218 1 O ALA A 217 N LEU A 132
SHEET 3 B 5 ARG A 188 ASN A 192 1 N VAL A 191 O LEU A 218
SHEET 4 B 5 ALA A 147 ASP A 151 1 N LEU A 150 O ILE A 190
SHEET 5 B 5 ILE A 167 SER A 168 1 O ILE A 167 N ILE A 149
SHEET 1 C 5 GLU A 265 LEU A 267 0
SHEET 2 C 5 GLN A 348 LEU A 352 1 O VAL A 349 N GLU A 265
SHEET 3 C 5 ARG A 324 VAL A 328 1 N LEU A 327 O ALA A 350
SHEET 4 C 5 THR A 283 ASP A 287 1 N LEU A 286 O VAL A 328
SHEET 5 C 5 ARG A 303 SER A 304 1 O ARG A 303 N ASP A 287
SHEET 1 D 5 THR A 378 ILE A 379 0
SHEET 2 D 5 VAL A 458 LEU A 461 1 O LEU A 460 N ILE A 379
SHEET 3 D 5 ARG A 432 THR A 436 1 N LEU A 435 O PHE A 459
SHEET 4 D 5 THR A 393 ASP A 397 1 N ARG A 394 O ARG A 432
SHEET 5 D 5 ALA A 413 TRP A 414 1 O ALA A 413 N ASP A 397
LINK C THR A 160 N MSE A 161 1555 1555 1.33
LINK C MSE A 161 N SER A 162 1555 1555 1.33
LINK C ASN A 336 N MSE A 337 1555 1555 1.33
LINK C MSE A 337 N SER A 338 1555 1555 1.33
LINK C GLN A 344 N MSE A 345 1555 1555 1.33
LINK C MSE A 345 N GLY A 346 1555 1555 1.33
LINK C ALA A 503 N MSE A 504 1555 1555 1.33
LINK C MSE A 504 N GLN A 505 1555 1555 1.33
SITE 1 AC1 7 CYS A 193 ALA A 194 GLY A 195 ARG A 196
SITE 2 AC1 7 THR A 197 ARG A 198 HOH A 784
SITE 1 AC2 8 ASN A 45 LEU A 46 PRO A 47 ARG A 50
SITE 2 AC2 8 GLU A 54 ARG A 58 HIS A 316 HOH A 733
CRYST1 88.348 114.476 69.438 90.00 90.00 90.00 P 21 21 2 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 0.011319 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008735 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014401 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
