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HEADER HYDROLASE 31-AUG-10 3OOS
TITLE THE STRUCTURE OF AN ALPHA/BETA FOLD FAMILY HYDROLASE FROM BACILLUS
TITLE 2 ANTHRACIS STR. STERNE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYDROLASE, ALPHA/BETA FOLD FAMILY;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_TAXID: 260799;
SOURCE 4 STRAIN: STERNE;
SOURCE 5 GENE: BAS2502, BA_2687, GBAA2687, GBAA_2687;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS APC67239.0, PROTEIN STRUCTURE INITIATIVE, PSI-2, STRUCTURAL GENOMICS,
KEYWDS 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, MEDICAL STRUCTURAL
KEYWDS 3 GENOMICS OF PATHOGENIC PROTOZOA, MSGPP, ALPHA/BETA FOLD FAMILY,
KEYWDS 4 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.FAN,K.TAN,L.BIGELOW,J.HAMILTON,H.LI,Y.ZHOU,S.CLANCY,K.BUCK,
AUTHOR 2 A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 10-NOV-10 3OOS 0
JRNL AUTH Y.FAN,K.TAN,L.BIGELOW,J.HAMILTON,H.LI,Y.ZHOU,S.CLANCY,
JRNL AUTH 2 K.BUCK,A.JOACHIMIAK
JRNL TITL THE STRUCTURE OF AN ALPHA/BETA FOLD FAMILY HYDROLASE FROM
JRNL TITL 2 BACILLUS ANTHRACIS STR. STERNE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 38732
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2040
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) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2719
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE SET COUNT : 139
REMARK 3 BIN FREE R VALUE : 0.2080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2227
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 414
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : 0.05000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.084
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.974
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2593 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3534 ; 0.897 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 348 ; 5.093 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;38.774 ;25.433
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 485 ;11.908 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;15.479 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 372 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1988 ; 0.004 ; 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): 1524 ; 0.408 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2505 ; 0.775 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1069 ; 1.299 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1000 ; 2.103 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2593 ; 0.533 ; 3.000
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 : 1
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 -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3391 21.7885 37.2034
REMARK 3 T TENSOR
REMARK 3 T11: 0.0034 T22: 0.0011
REMARK 3 T33: 0.0045 T12: -0.0015
REMARK 3 T13: 0.0006 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.1669 L22: 0.0818
REMARK 3 L33: 0.1232 L12: -0.0457
REMARK 3 L13: 0.0633 L23: 0.0136
REMARK 3 S TENSOR
REMARK 3 S11: -0.0026 S12: 0.0009 S13: -0.0136
REMARK 3 S21: -0.0022 S22: 0.0026 S23: 0.0048
REMARK 3 S31: -0.0069 S32: 0.0010 S33: 0.0000
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OOS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061384.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40780
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 56.0300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.18100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 12.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/ARP/WARP/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M HEPES
REMARK 280 PH7.5, 16%W/V PEG4000, 10%W/V ISOPROPANOL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
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 36.85850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.41950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.93350
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.85850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.41950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.93350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.85850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.41950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.93350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.85850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.41950
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.93350
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A 468 LIES ON A SPECIAL POSITION.
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 TYR A 31 50.48 -150.73
REMARK 500 SER A 98 -117.90 62.23
REMARK 500 ALA A 111 45.29 -144.32
REMARK 500 ALA A 123 -168.73 -114.32
REMARK 500 ASP A 211 114.22 -167.53
REMARK 500 GLN A 233 -73.22 -93.93
REMARK 500 ASN A 258 -98.27 -94.64
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 SO4 A 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 283
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC67239.0 RELATED DB: TARGETDB
DBREF 3OOS A 1 277 UNP Q81PV7 Q81PV7_BACAN 1 277
SEQADV 3OOS ALA A 0 UNP Q81PV7 EXPRESSION TAG
SEQRES 1 A 278 ALA MSE TRP THR THR ASN ILE ILE LYS THR PRO ARG GLY
SEQRES 2 A 278 LYS PHE GLU TYR PHE LEU LYS GLY GLU GLY PRO PRO LEU
SEQRES 3 A 278 CYS VAL THR HIS LEU TYR SER GLU TYR ASN ASP ASN GLY
SEQRES 4 A 278 ASN THR PHE ALA ASN PRO PHE THR ASP HIS TYR SER VAL
SEQRES 5 A 278 TYR LEU VAL ASN LEU LYS GLY CYS GLY ASN SER ASP SER
SEQRES 6 A 278 ALA LYS ASN ASP SER GLU TYR SER MSE THR GLU THR ILE
SEQRES 7 A 278 LYS ASP LEU GLU ALA ILE ARG GLU ALA LEU TYR ILE ASN
SEQRES 8 A 278 LYS TRP GLY PHE ALA GLY HIS SER ALA GLY GLY MSE LEU
SEQRES 9 A 278 ALA LEU VAL TYR ALA THR GLU ALA GLN GLU SER LEU THR
SEQRES 10 A 278 LYS ILE ILE VAL GLY GLY ALA ALA ALA SER LYS GLU TYR
SEQRES 11 A 278 ALA SER HIS LYS ASP SER ILE TYR CYS SER LYS ASN VAL
SEQRES 12 A 278 LYS PHE ASN ARG ILE VAL SER ILE MSE ASN ALA LEU ASN
SEQRES 13 A 278 ASP ASP SER THR VAL GLN GLU GLU ARG LYS ALA LEU SER
SEQRES 14 A 278 ARG GLU TRP ALA LEU MSE SER PHE TYR SER GLU GLU LYS
SEQRES 15 A 278 LEU GLU GLU ALA LEU LYS LEU PRO ASN SER GLY LYS THR
SEQRES 16 A 278 VAL GLY ASN ARG LEU ASN TYR PHE ARG GLN VAL GLU TYR
SEQRES 17 A 278 LYS ASP TYR ASP VAL ARG GLN LYS LEU LYS PHE VAL LYS
SEQRES 18 A 278 ILE PRO SER PHE ILE TYR CYS GLY LYS HIS ASP VAL GLN
SEQRES 19 A 278 CYS PRO TYR ILE PHE SER CYS GLU ILE ALA ASN LEU ILE
SEQRES 20 A 278 PRO ASN ALA THR LEU THR LYS PHE GLU GLU SER ASN HIS
SEQRES 21 A 278 ASN PRO PHE VAL GLU GLU ILE ASP LYS PHE ASN GLN PHE
SEQRES 22 A 278 VAL ASN ASP THR LEU
MODRES 3OOS MSE A 1 MET SELENOMETHIONINE
MODRES 3OOS MSE A 73 MET SELENOMETHIONINE
MODRES 3OOS MSE A 102 MET SELENOMETHIONINE
MODRES 3OOS MSE A 151 MET SELENOMETHIONINE
MODRES 3OOS MSE A 174 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 73 16
HET MSE A 102 8
HET MSE A 151 8
HET MSE A 174 8
HET SO4 A 278 5
HET GOL A 279 6
HET PG4 A 280 13
HET PG4 A 281 13
HET PG4 A 282 13
HET GOL A 283 6
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 SO4 O4 S 2-
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 PG4 3(C8 H18 O5)
FORMUL 8 HOH *414(H2 O)
HELIX 1 1 ALA A 42 HIS A 48 5 7
HELIX 2 2 ASN A 67 TYR A 71 5 5
HELIX 3 3 SER A 72 LEU A 87 1 16
HELIX 4 4 SER A 98 GLN A 112 1 15
HELIX 5 5 SER A 126 HIS A 132 5 7
HELIX 6 6 LYS A 143 ASN A 155 1 13
HELIX 7 7 VAL A 160 PHE A 176 1 17
HELIX 8 8 SER A 178 LEU A 186 1 9
HELIX 9 9 VAL A 195 VAL A 205 1 11
HELIX 10 10 GLU A 206 TYR A 210 5 5
HELIX 11 11 VAL A 212 LYS A 217 1 6
HELIX 12 12 PRO A 235 ILE A 246 1 12
HELIX 13 13 ASN A 260 GLU A 265 1 6
HELIX 14 14 GLU A 265 THR A 276 1 12
SHEET 1 A 8 THR A 3 THR A 9 0
SHEET 2 A 8 GLY A 12 LYS A 19 -1 O LEU A 18 N THR A 3
SHEET 3 A 8 SER A 50 VAL A 54 -1 O LEU A 53 N PHE A 17
SHEET 4 A 8 PRO A 24 VAL A 27 1 N LEU A 25 O TYR A 52
SHEET 5 A 8 TRP A 92 HIS A 97 1 O GLY A 93 N CYS A 26
SHEET 6 A 8 LEU A 115 GLY A 121 1 O GLY A 121 N GLY A 96
SHEET 7 A 8 SER A 223 GLY A 228 1 O PHE A 224 N ILE A 118
SHEET 8 A 8 ALA A 249 PHE A 254 1 O THR A 250 N ILE A 225
SHEET 1 B 2 SER A 32 GLU A 33 0
SHEET 2 B 2 LYS A 193 THR A 194 -1 O LYS A 193 N GLU A 33
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N TRP A 2 1555 1555 1.33
LINK C SER A 72 N AMSE A 73 1555 1555 1.33
LINK C SER A 72 N BMSE A 73 1555 1555 1.33
LINK C AMSE A 73 N ATHR A 74 1555 1555 1.33
LINK C BMSE A 73 N BTHR A 74 1555 1555 1.33
LINK C GLY A 101 N MSE A 102 1555 1555 1.33
LINK C MSE A 102 N LEU A 103 1555 1555 1.33
LINK C ILE A 150 N MSE A 151 1555 1555 1.33
LINK C MSE A 151 N ASN A 152 1555 1555 1.33
LINK C LEU A 173 N MSE A 174 1555 1555 1.33
LINK C MSE A 174 N SER A 175 1555 1555 1.33
SITE 1 AC1 8 HIS A 29 TYR A 31 SER A 98 ALA A 99
SITE 2 AC1 8 GLN A 233 HIS A 259 PG4 A 281 HOH A 598
SITE 1 AC2 10 ARG A 146 SER A 149 ALA A 153 GLU A 163
SITE 2 AC2 10 THR A 250 LEU A 251 HOH A 487 HOH A 639
SITE 3 AC2 10 HOH A 643 HOH A 647
SITE 1 AC3 5 TYR A 137 ARG A 164 SER A 168 TRP A 171
SITE 2 AC3 5 HOH A 326
SITE 1 AC4 11 TYR A 31 SER A 98 TYR A 129 TYR A 137
SITE 2 AC4 11 PHE A 202 ARG A 203 TYR A 207 GLN A 233
SITE 3 AC4 11 CYS A 234 SO4 A 278 HOH A 338
SITE 1 AC5 9 GLU A 33 ASN A 35 SER A 191 GLY A 192
SITE 2 AC5 9 LYS A 193 GOL A 283 HOH A 500 HOH A 545
SITE 3 AC5 9 HOH A 548
SITE 1 AC6 5 ASN A 190 GLY A 192 PG4 A 282 HOH A 542
SITE 2 AC6 5 HOH A 545
CRYST1 73.717 80.839 113.867 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 0.013565 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012370 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008782 0.00000
TER 2456 LEU A 277
MASTER 325 0 11 14 10 0 15 6 2697 1 115 22
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