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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 29-JUL-07 2QRU
TITLE CRYSTAL STRUCTURE OF AN ALPHA/BETA HYDROLASE SUPERFAMILY
TITLE 2 PROTEIN FROM ENTEROCOCCUS FAECALIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS V583;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: V583;
SOURCE 5 ATCC: 700802;
SOURCE 6 GENE: EF_0381;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ENTEROCOCCUS FAECALIS, ALPHA/BETA-HYDROLASE, STRUCTURAL
KEYWDS 2 GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST
KEYWDS 3 CENTER FOR STRUCTURAL GENOMICS, MCSG, STRUCTURAL GENOMICS,
KEYWDS 4 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.CUFF,L.VOLKART,S.MOY,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 11-SEP-07 2QRU 0
JRNL AUTH M.E.CUFF,L.VOLKART,S.MOY,A.JOACHIMIAK
JRNL TITL STRUCTURE OF AN ALPHA/BETA HYDROLASE SUPERFAMILY
JRNL TITL 2 PROTEIN FROM ENTEROCOCCUS FAECALIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 33.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 35870
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1804
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2372
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2675
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.84000
REMARK 3 B22 (A**2) : -0.88000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.46000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.285
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2376 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3238 ; 1.350 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 292 ; 5.894 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 108 ;39.407 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 402 ;12.664 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;17.474 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 359 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1815 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1243 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1657 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 301 ; 0.151 ; 0.200
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): 50 ; 0.144 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.218 ; 0.200
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): 1462 ; 0.815 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2332 ; 1.263 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1037 ; 2.044 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 906 ; 3.080 ; 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 : 0
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 2 A 272
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2237 22.0434 12.9173
REMARK 3 T TENSOR
REMARK 3 T11: -0.1228 T22: -0.0675
REMARK 3 T33: -0.0826 T12: -0.0512
REMARK 3 T13: 0.0041 T23: -0.0596
REMARK 3 L TENSOR
REMARK 3 L11: 1.0796 L22: 2.9093
REMARK 3 L33: 1.9677 L12: 0.1059
REMARK 3 L13: -0.6147 L23: 0.7106
REMARK 3 S TENSOR
REMARK 3 S11: 0.1166 S12: 0.0254 S13: -0.0112
REMARK 3 S21: 0.3019 S22: -0.3421 S23: 0.3630
REMARK 3 S31: 0.0170 S32: -0.1425 S33: 0.2255
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2QRU COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB043975.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
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) : 0.97878, 0.97894
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36066
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.49100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.920
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: HKL-3000, SHELXD, SHELXE, MLPHARE, DM, SOLVE/
REMARK 200 RESOLVE, ARP/WARP, CCP4, O, COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M MGCL2, 10% PEG 6000, 0.1M
REMARK 280 TRIS-HCL PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 49.67600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.20650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.67600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.20650
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 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 300
REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT ASSEMBLY HAS
REMARK 300 NOT BEEN DETERMINED EXPERIMENTALLY AND THAT THE MONOMERIC
REMARK 300 PREDICTION IS BASED ON CRYSTAL PACKING.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
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 412 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 SER A -1
REMARK 465 ASN A 0
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
REMARK 500 O HOH A 364 O HOH A 554 2.12
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 102 -112.40 54.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC28784 RELATED DB: TARGETDB
DBREF 2QRU A 2 272 UNP Q838Q5 Q838Q5_ENTFA 2 272
SEQADV 2QRU SER A -1 UNP Q838Q5 EXPRESSION TAG
SEQADV 2QRU ASN A 0 UNP Q838Q5 EXPRESSION TAG
SEQADV 2QRU ALA A 1 UNP Q838Q5 EXPRESSION TAG
SEQRES 1 A 274 SER ASN ALA HIS LEU LYS ASN ASN GLN THR LEU ALA ASN
SEQRES 2 A 274 GLY ALA THR VAL THR ILE TYR PRO THR THR THR GLU PRO
SEQRES 3 A 274 THR ASN TYR VAL VAL TYR LEU HIS GLY GLY GLY MSE ILE
SEQRES 4 A 274 TYR GLY THR LYS SER ASP LEU PRO GLU GLU LEU LYS GLU
SEQRES 5 A 274 LEU PHE THR SER ASN GLY TYR THR VAL LEU ALA LEU ASP
SEQRES 6 A 274 TYR LEU LEU ALA PRO ASN THR LYS ILE ASP HIS ILE LEU
SEQRES 7 A 274 ARG THR LEU THR GLU THR PHE GLN LEU LEU ASN GLU GLU
SEQRES 8 A 274 ILE ILE GLN ASN GLN SER PHE GLY LEU CYS GLY ARG SER
SEQRES 9 A 274 ALA GLY GLY TYR LEU MSE LEU GLN LEU THR LYS GLN LEU
SEQRES 10 A 274 GLN THR LEU ASN LEU THR PRO GLN PHE LEU VAL ASN PHE
SEQRES 11 A 274 TYR GLY TYR THR ASP LEU GLU PHE ILE LYS GLU PRO ARG
SEQRES 12 A 274 LYS LEU LEU LYS GLN ALA ILE SER ALA LYS GLU ILE ALA
SEQRES 13 A 274 ALA ILE ASP GLN THR LYS PRO VAL TRP ASP ASP PRO PHE
SEQRES 14 A 274 LEU SER ARG TYR LEU LEU TYR HIS TYR SER ILE GLN GLN
SEQRES 15 A 274 ALA LEU LEU PRO HIS PHE TYR GLY LEU PRO GLU ASN GLY
SEQRES 16 A 274 ASP TRP SER ALA TYR ALA LEU SER ASP GLU THR LEU LYS
SEQRES 17 A 274 THR PHE PRO PRO CYS PHE SER THR ALA SER SER SER ASP
SEQRES 18 A 274 GLU GLU VAL PRO PHE ARG TYR SER LYS LYS ILE GLY ARG
SEQRES 19 A 274 THR ILE PRO GLU SER THR PHE LYS ALA VAL TYR TYR LEU
SEQRES 20 A 274 GLU HIS ASP PHE LEU LYS GLN THR LYS ASP PRO SER VAL
SEQRES 21 A 274 ILE THR LEU PHE GLU GLN LEU ASP SER TRP LEU LYS GLU
SEQRES 22 A 274 ARG
MODRES 2QRU MSE A 36 MET SELENOMETHIONINE
MODRES 2QRU MSE A 108 MET SELENOMETHIONINE
HET MSE A 36 8
HET MSE A 108 8
HET PO4 A 273 5
HET EDO A 274 4
HET EDO A 275 4
HET EDO A 276 4
HET EDO A 277 4
HET EDO A 278 4
HET EDO A 279 4
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 PO4 O4 P 3-
FORMUL 3 EDO 6(C2 H6 O2)
FORMUL 9 HOH *359(H2 O)
HELIX 1 1 THR A 40 LEU A 44 5 5
HELIX 2 2 PRO A 45 SER A 54 1 10
HELIX 3 3 LYS A 71 ILE A 90 1 20
HELIX 4 4 SER A 102 LEU A 118 1 17
HELIX 5 5 LEU A 134 GLU A 139 5 6
HELIX 6 6 ALA A 150 ALA A 154 5 5
HELIX 7 7 ARG A 170 GLN A 180 1 11
HELIX 8 8 LEU A 182 GLY A 188 1 7
HELIX 9 9 TRP A 195 ALA A 199 5 5
HELIX 10 10 SER A 201 THR A 207 1 7
HELIX 11 11 PHE A 224 ILE A 234 1 11
HELIX 12 12 ASP A 248 THR A 253 5 6
HELIX 13 13 ASP A 255 GLU A 271 1 17
SHEET 1 A 8 ASN A 5 THR A 8 0
SHEET 2 A 8 THR A 14 TYR A 18 -1 O ILE A 17 N ASN A 5
SHEET 3 A 8 TYR A 57 LEU A 62 -1 O ALA A 61 N THR A 16
SHEET 4 A 8 ASN A 26 LEU A 31 1 N VAL A 28 O LEU A 60
SHEET 5 A 8 PHE A 96 ARG A 101 1 O CYS A 99 N LEU A 31
SHEET 6 A 8 LEU A 125 PHE A 128 1 O PHE A 128 N GLY A 100
SHEET 7 A 8 CYS A 211 SER A 216 1 O PHE A 212 N ASN A 127
SHEET 8 A 8 THR A 238 VAL A 242 1 O THR A 238 N SER A 213
CISPEP 1 GLU A 23 PRO A 24 0 -2.40
CISPEP 2 ALA A 67 PRO A 68 0 -0.89
CRYST1 99.352 50.413 64.683 90.00 110.27 90.00 C 1 2 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 0.010065 0.000000 0.003717 0.00000
SCALE2 0.000000 0.019836 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016480 0.00000
TER 2288 ARG A 272
MASTER 299 0 9 13 8 0 0 6 2675 1 45 22
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