HEADER OXIDOREDUCTASE 01-NOV-05 2EW2
TITLE CRYSTAL STRUCTURE OF THE PUTATIVE 2-DEHYDROPANTOATE 2-REDUCTASE FROM
TITLE 2 ENTEROCOCCUS FAECALIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-DEHYDROPANTOATE 2-REDUCTASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.169;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_TAXID: 226185;
SOURCE 4 STRAIN: V583;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ALPHA-STRUCTURE, ALPHA-BETA STRUCTURE, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,M.ZHOU,S.MOY,S.CLANCY,F.COLLART,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 3 13-JUL-11 2EW2 1 VERSN
REVDAT 2 24-FEB-09 2EW2 1 VERSN
REVDAT 1 13-DEC-05 2EW2 0
JRNL AUTH Y.KIM,M.ZHOU,S.MOY,S.CLANCY,F.COLLART,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF THE PUTATIVE 2-DEHYDROPANTOATE
JRNL TITL 2 2-REDUCTASE FROM ENTEROCOCCUS FAECALIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0000
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 47668
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5345
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2144
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 249
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4845
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.34000
REMARK 3 B22 (A**2) : -0.56000
REMARK 3 B33 (A**2) : -1.78000
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): 0.177
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.378
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5137 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6995 ; 1.204 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 667 ; 5.414 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 225 ;42.486 ;25.778
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 907 ;13.980 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;22.012 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 788 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3898 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2450 ; 0.199 ; 0.200
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): 428 ; 0.142 ; 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): 31 ; 0.172 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.163 ; 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): 3353 ; 0.781 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5222 ; 1.209 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2058 ; 2.178 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1773 ; 3.392 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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: NULL
REMARK 4
REMARK 4 2EW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-05.
REMARK 100 THE RCSB ID CODE IS RCSB035162.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-05
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 : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 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 : SBCCOLLECT, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53058
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 33.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 11.700
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 59.8
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.160
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS/HCL, 30% PEG400, 200MM
REMARK 280 MGCL2, PH 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 44.58250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.37700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.58000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.37700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.58250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.58000
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: 2270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 SER B -2
REMARK 465 ASN B -1
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 8 43.34 -99.21
REMARK 500 THR A 194 -81.52 -117.32
REMARK 500 ASP A 203 81.09 51.57
REMARK 500 ILE A 278 -97.42 -129.02
REMARK 500 ALA B 8 39.69 -96.52
REMARK 500 THR B 194 -81.63 -113.42
REMARK 500 ASP B 203 76.96 59.23
REMARK 500 ILE B 278 -94.76 -126.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 700 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B 360 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH B 380 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH B 524 DISTANCE = 5.70 ANGSTROMS
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 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 308 OE1
REMARK 620 2 HOH A 553 O 91.2
REMARK 620 3 HOH A 534 O 92.5 93.7
REMARK 620 4 HOH A 657 O 89.3 88.0 177.5
REMARK 620 5 HOH A 659 O 82.5 170.1 94.2 84.3
REMARK 620 6 HOH B 367 O 173.0 95.3 89.6 88.4 90.7
REMARK 620 N 1 2 3 4 5
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC29419 RELATED DB: TARGETDB
DBREF 2EW2 A 1 313 UNP Q831Q5 Q831Q5_ENTFA 1 313
DBREF 2EW2 B 1 313 UNP Q831Q5 Q831Q5_ENTFA 1 313
SEQADV 2EW2 SER A -2 UNP Q831Q5 CLONING ARTIFACT
SEQADV 2EW2 ASN A -1 UNP Q831Q5 CLONING ARTIFACT
SEQADV 2EW2 ALA A 0 UNP Q831Q5 CLONING ARTIFACT
SEQADV 2EW2 MSE A 1 UNP Q831Q5 MET 1 MODIFIED RESIDUE
SEQADV 2EW2 MSE A 11 UNP Q831Q5 MET 11 MODIFIED RESIDUE
SEQADV 2EW2 MSE A 18 UNP Q831Q5 MET 18 MODIFIED RESIDUE
SEQADV 2EW2 MSE A 87 UNP Q831Q5 MET 87 MODIFIED RESIDUE
SEQADV 2EW2 MSE A 94 UNP Q831Q5 MET 94 MODIFIED RESIDUE
SEQADV 2EW2 MSE A 129 UNP Q831Q5 MET 129 MODIFIED RESIDUE
SEQADV 2EW2 MSE A 262 UNP Q831Q5 MET 262 MODIFIED RESIDUE
SEQADV 2EW2 MSE A 298 UNP Q831Q5 MET 298 MODIFIED RESIDUE
SEQADV 2EW2 SER B -2 UNP Q831Q5 CLONING ARTIFACT
SEQADV 2EW2 ASN B -1 UNP Q831Q5 CLONING ARTIFACT
SEQADV 2EW2 ALA B 0 UNP Q831Q5 CLONING ARTIFACT
SEQADV 2EW2 MSE B 1 UNP Q831Q5 MET 1 MODIFIED RESIDUE
SEQADV 2EW2 MSE B 11 UNP Q831Q5 MET 11 MODIFIED RESIDUE
SEQADV 2EW2 MSE B 18 UNP Q831Q5 MET 18 MODIFIED RESIDUE
SEQADV 2EW2 MSE B 87 UNP Q831Q5 MET 87 MODIFIED RESIDUE
SEQADV 2EW2 MSE B 94 UNP Q831Q5 MET 94 MODIFIED RESIDUE
SEQADV 2EW2 MSE B 129 UNP Q831Q5 MET 129 MODIFIED RESIDUE
SEQADV 2EW2 MSE B 262 UNP Q831Q5 MET 262 MODIFIED RESIDUE
SEQADV 2EW2 MSE B 298 UNP Q831Q5 MET 298 MODIFIED RESIDUE
SEQRES 1 A 316 SER ASN ALA MSE LYS ILE ALA ILE ALA GLY ALA GLY ALA
SEQRES 2 A 316 MSE GLY SER ARG LEU GLY ILE MSE LEU HIS GLN GLY GLY
SEQRES 3 A 316 ASN ASP VAL THR LEU ILE ASP GLN TRP PRO ALA HIS ILE
SEQRES 4 A 316 GLU ALA ILE ARG LYS ASN GLY LEU ILE ALA ASP PHE ASN
SEQRES 5 A 316 GLY GLU GLU VAL VAL ALA ASN LEU PRO ILE PHE SER PRO
SEQRES 6 A 316 GLU GLU ILE ASP HIS GLN ASN GLU GLN VAL ASP LEU ILE
SEQRES 7 A 316 ILE ALA LEU THR LYS ALA GLN GLN LEU ASP ALA MSE PHE
SEQRES 8 A 316 LYS ALA ILE GLN PRO MSE ILE THR GLU LYS THR TYR VAL
SEQRES 9 A 316 LEU CYS LEU LEU ASN GLY LEU GLY HIS GLU ASP VAL LEU
SEQRES 10 A 316 GLU LYS TYR VAL PRO LYS GLU ASN ILE LEU VAL GLY ILE
SEQRES 11 A 316 THR MSE TRP THR ALA GLY LEU GLU GLY PRO GLY ARG VAL
SEQRES 12 A 316 LYS LEU LEU GLY ASP GLY GLU ILE GLU LEU GLU ASN ILE
SEQRES 13 A 316 ASP PRO SER GLY LYS LYS PHE ALA LEU GLU VAL VAL ASP
SEQRES 14 A 316 VAL PHE GLN LYS ALA GLY LEU ASN PRO SER TYR SER SER
SEQRES 15 A 316 ASN VAL ARG TYR SER ILE TRP ARG LYS ALA CYS VAL ASN
SEQRES 16 A 316 GLY THR LEU ASN GLY LEU CYS THR ILE LEU ASP CYS ASN
SEQRES 17 A 316 ILE ALA GLU PHE GLY ALA LEU PRO VAL SER GLU SER LEU
SEQRES 18 A 316 VAL LYS THR LEU ILE SER GLU PHE ALA ALA VAL ALA GLU
SEQRES 19 A 316 LYS GLU ALA ILE TYR LEU ASP GLN ALA GLU VAL TYR THR
SEQRES 20 A 316 HIS ILE VAL GLN THR TYR ASP PRO ASN GLY ILE GLY LEU
SEQRES 21 A 316 HIS TYR PRO SER MSE TYR GLN ASP LEU ILE LYS ASN HIS
SEQRES 22 A 316 ARG LEU THR GLU ILE ASP TYR ILE ASN GLY ALA VAL TRP
SEQRES 23 A 316 ARG LYS GLY GLN LYS TYR ASN VAL ALA THR PRO PHE CYS
SEQRES 24 A 316 ALA MSE LEU THR GLN LEU VAL HIS GLY LYS GLU GLU LEU
SEQRES 25 A 316 LEU GLY ALA LYS
SEQRES 1 B 316 SER ASN ALA MSE LYS ILE ALA ILE ALA GLY ALA GLY ALA
SEQRES 2 B 316 MSE GLY SER ARG LEU GLY ILE MSE LEU HIS GLN GLY GLY
SEQRES 3 B 316 ASN ASP VAL THR LEU ILE ASP GLN TRP PRO ALA HIS ILE
SEQRES 4 B 316 GLU ALA ILE ARG LYS ASN GLY LEU ILE ALA ASP PHE ASN
SEQRES 5 B 316 GLY GLU GLU VAL VAL ALA ASN LEU PRO ILE PHE SER PRO
SEQRES 6 B 316 GLU GLU ILE ASP HIS GLN ASN GLU GLN VAL ASP LEU ILE
SEQRES 7 B 316 ILE ALA LEU THR LYS ALA GLN GLN LEU ASP ALA MSE PHE
SEQRES 8 B 316 LYS ALA ILE GLN PRO MSE ILE THR GLU LYS THR TYR VAL
SEQRES 9 B 316 LEU CYS LEU LEU ASN GLY LEU GLY HIS GLU ASP VAL LEU
SEQRES 10 B 316 GLU LYS TYR VAL PRO LYS GLU ASN ILE LEU VAL GLY ILE
SEQRES 11 B 316 THR MSE TRP THR ALA GLY LEU GLU GLY PRO GLY ARG VAL
SEQRES 12 B 316 LYS LEU LEU GLY ASP GLY GLU ILE GLU LEU GLU ASN ILE
SEQRES 13 B 316 ASP PRO SER GLY LYS LYS PHE ALA LEU GLU VAL VAL ASP
SEQRES 14 B 316 VAL PHE GLN LYS ALA GLY LEU ASN PRO SER TYR SER SER
SEQRES 15 B 316 ASN VAL ARG TYR SER ILE TRP ARG LYS ALA CYS VAL ASN
SEQRES 16 B 316 GLY THR LEU ASN GLY LEU CYS THR ILE LEU ASP CYS ASN
SEQRES 17 B 316 ILE ALA GLU PHE GLY ALA LEU PRO VAL SER GLU SER LEU
SEQRES 18 B 316 VAL LYS THR LEU ILE SER GLU PHE ALA ALA VAL ALA GLU
SEQRES 19 B 316 LYS GLU ALA ILE TYR LEU ASP GLN ALA GLU VAL TYR THR
SEQRES 20 B 316 HIS ILE VAL GLN THR TYR ASP PRO ASN GLY ILE GLY LEU
SEQRES 21 B 316 HIS TYR PRO SER MSE TYR GLN ASP LEU ILE LYS ASN HIS
SEQRES 22 B 316 ARG LEU THR GLU ILE ASP TYR ILE ASN GLY ALA VAL TRP
SEQRES 23 B 316 ARG LYS GLY GLN LYS TYR ASN VAL ALA THR PRO PHE CYS
SEQRES 24 B 316 ALA MSE LEU THR GLN LEU VAL HIS GLY LYS GLU GLU LEU
SEQRES 25 B 316 LEU GLY ALA LYS
MODRES 2EW2 MSE A 1 MET SELENOMETHIONINE
MODRES 2EW2 MSE A 11 MET SELENOMETHIONINE
MODRES 2EW2 MSE A 18 MET SELENOMETHIONINE
MODRES 2EW2 MSE A 87 MET SELENOMETHIONINE
MODRES 2EW2 MSE A 94 MET SELENOMETHIONINE
MODRES 2EW2 MSE A 129 MET SELENOMETHIONINE
MODRES 2EW2 MSE A 262 MET SELENOMETHIONINE
MODRES 2EW2 MSE A 298 MET SELENOMETHIONINE
MODRES 2EW2 MSE B 1 MET SELENOMETHIONINE
MODRES 2EW2 MSE B 11 MET SELENOMETHIONINE
MODRES 2EW2 MSE B 18 MET SELENOMETHIONINE
MODRES 2EW2 MSE B 87 MET SELENOMETHIONINE
MODRES 2EW2 MSE B 94 MET SELENOMETHIONINE
MODRES 2EW2 MSE B 129 MET SELENOMETHIONINE
MODRES 2EW2 MSE B 262 MET SELENOMETHIONINE
MODRES 2EW2 MSE B 298 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 11 8
HET MSE A 18 8
HET MSE A 87 8
HET MSE A 94 8
HET MSE A 129 8
HET MSE A 262 8
HET MSE A 298 8
HET MSE B 1 8
HET MSE B 11 8
HET MSE B 18 8
HET MSE B 87 8
HET MSE B 94 8
HET MSE B 129 16
HET MSE B 262 8
HET MSE B 298 8
HET SO4 A 501 5
HET MG A 502 1
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 3 SO4 O4 S 2-
FORMUL 4 MG MG 2+
FORMUL 5 HOH *450(H2 O)
HELIX 1 1 GLY A 9 GLY A 22 1 14
HELIX 2 2 TRP A 32 GLY A 43 1 12
HELIX 3 3 SER A 61 ILE A 65 5 5
HELIX 4 4 LYS A 80 GLN A 92 1 13
HELIX 5 5 PRO A 93 ILE A 95 5 3
HELIX 6 6 HIS A 110 GLU A 115 1 6
HELIX 7 7 PRO A 119 GLU A 121 5 3
HELIX 8 8 ASP A 154 SER A 156 5 3
HELIX 9 9 GLY A 157 ALA A 171 1 15
HELIX 10 10 ASN A 180 GLY A 193 1 14
HELIX 11 11 THR A 194 ASP A 203 1 10
HELIX 12 12 ASN A 205 ALA A 211 1 7
HELIX 13 13 VAL A 214 GLU A 233 1 20
HELIX 14 14 ASP A 238 THR A 249 1 12
HELIX 15 15 PRO A 260 ILE A 267 1 8
HELIX 16 16 GLU A 274 TYR A 277 5 4
HELIX 17 17 ILE A 278 ASN A 290 1 13
HELIX 18 18 THR A 293 LEU A 310 1 18
HELIX 19 19 GLY B 9 GLY B 22 1 14
HELIX 20 20 TRP B 32 GLY B 43 1 12
HELIX 21 21 SER B 61 ILE B 65 5 5
HELIX 22 22 LYS B 80 GLN B 92 1 13
HELIX 23 23 PRO B 93 ILE B 95 5 3
HELIX 24 24 HIS B 110 GLU B 115 1 6
HELIX 25 25 PRO B 119 GLU B 121 5 3
HELIX 26 26 ASP B 154 SER B 156 5 3
HELIX 27 27 GLY B 157 ALA B 171 1 15
HELIX 28 28 ASN B 180 GLY B 193 1 14
HELIX 29 29 THR B 194 ASP B 203 1 10
HELIX 30 30 ASN B 205 LEU B 212 1 8
HELIX 31 31 VAL B 214 GLU B 233 1 20
HELIX 32 32 ASP B 238 TYR B 250 1 13
HELIX 33 33 PRO B 260 ILE B 267 1 8
HELIX 34 34 GLU B 274 TYR B 277 5 4
HELIX 35 35 ILE B 278 ASN B 290 1 13
HELIX 36 36 THR B 293 GLY B 311 1 19
SHEET 1 A 8 ILE A 59 PHE A 60 0
SHEET 2 A 8 ASP A 25 ILE A 29 1 N LEU A 28 O PHE A 60
SHEET 3 A 8 LYS A 2 ALA A 6 1 N ILE A 3 O ASP A 25
SHEET 4 A 8 LEU A 74 ALA A 77 1 O LEU A 74 N ALA A 4
SHEET 5 A 8 TYR A 100 CYS A 103 1 O LEU A 102 N ILE A 75
SHEET 6 A 8 ILE A 123 THR A 128 1 O LEU A 124 N VAL A 101
SHEET 7 A 8 ILE A 148 ASN A 152 -1 O GLU A 151 N VAL A 125
SHEET 8 A 8 PRO A 175 TYR A 177 1 O SER A 176 N LEU A 150
SHEET 1 B 4 GLU A 51 ALA A 55 0
SHEET 2 B 4 LEU A 44 PHE A 48 -1 N ALA A 46 O VAL A 53
SHEET 3 B 4 ARG A 139 LEU A 142 1 O LEU A 142 N ASP A 47
SHEET 4 B 4 GLY A 133 GLY A 136 -1 N GLY A 133 O LYS A 141
SHEET 1 C 8 ILE B 59 PHE B 60 0
SHEET 2 C 8 ASP B 25 ILE B 29 1 N LEU B 28 O PHE B 60
SHEET 3 C 8 LYS B 2 ALA B 6 1 N ILE B 5 O THR B 27
SHEET 4 C 8 LEU B 74 ALA B 77 1 O ILE B 76 N ALA B 6
SHEET 5 C 8 TYR B 100 CYS B 103 1 O LEU B 102 N ILE B 75
SHEET 6 C 8 ILE B 123 THR B 128 1 O LEU B 124 N VAL B 101
SHEET 7 C 8 ILE B 148 ASN B 152 -1 O GLU B 151 N VAL B 125
SHEET 8 C 8 PRO B 175 TYR B 177 1 O SER B 176 N LEU B 150
SHEET 1 D 4 GLU B 51 ALA B 55 0
SHEET 2 D 4 LEU B 44 PHE B 48 -1 N ALA B 46 O VAL B 53
SHEET 3 D 4 ARG B 139 LEU B 142 1 O LEU B 142 N ASP B 47
SHEET 4 D 4 GLY B 133 GLY B 136 -1 N GLY B 133 O LYS B 141
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C ALA A 10 N MSE A 11 1555 1555 1.34
LINK C MSE A 11 N GLY A 12 1555 1555 1.33
LINK C ILE A 17 N MSE A 18 1555 1555 1.34
LINK C MSE A 18 N LEU A 19 1555 1555 1.34
LINK C ALA A 86 N MSE A 87 1555 1555 1.33
LINK C MSE A 87 N PHE A 88 1555 1555 1.33
LINK C PRO A 93 N MSE A 94 1555 1555 1.33
LINK C MSE A 94 N ILE A 95 1555 1555 1.34
LINK C THR A 128 N MSE A 129 1555 1555 1.33
LINK C MSE A 129 N TRP A 130 1555 1555 1.33
LINK C SER A 261 N MSE A 262 1555 1555 1.33
LINK C MSE A 262 N TYR A 263 1555 1555 1.33
LINK C ALA A 297 N MSE A 298 1555 1555 1.32
LINK C MSE A 298 N LEU A 299 1555 1555 1.33
LINK MG MG A 502 OE1 GLU A 308 1555 1555 2.14
LINK MG MG A 502 O HOH A 553 1555 1555 2.06
LINK MG MG A 502 O HOH A 534 1555 1555 2.21
LINK MG MG A 502 O HOH A 657 1555 1555 2.09
LINK MG MG A 502 O HOH A 659 1555 1555 2.21
LINK C ALA B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C ALA B 10 N MSE B 11 1555 1555 1.33
LINK C MSE B 11 N GLY B 12 1555 1555 1.33
LINK C ILE B 17 N MSE B 18 1555 1555 1.33
LINK C MSE B 18 N LEU B 19 1555 1555 1.34
LINK C ALA B 86 N MSE B 87 1555 1555 1.33
LINK C MSE B 87 N PHE B 88 1555 1555 1.33
LINK C PRO B 93 N MSE B 94 1555 1555 1.34
LINK C MSE B 94 N ILE B 95 1555 1555 1.33
LINK C THR B 128 N BMSE B 129 1555 1555 1.33
LINK C THR B 128 N AMSE B 129 1555 1555 1.33
LINK C BMSE B 129 N TRP B 130 1555 1555 1.33
LINK C AMSE B 129 N TRP B 130 1555 1555 1.33
LINK C SER B 261 N MSE B 262 1555 1555 1.34
LINK C MSE B 262 N TYR B 263 1555 1555 1.33
LINK C ALA B 297 N MSE B 298 1555 1555 1.33
LINK C MSE B 298 N LEU B 299 1555 1555 1.32
LINK MG MG A 502 O HOH B 367 1555 2674 2.21
SITE 1 AC1 3 ASP A 25 ASP B 47 GLU B 135
SITE 1 AC2 6 GLU A 308 HOH A 534 HOH A 553 HOH A 657
SITE 2 AC2 6 HOH A 659 HOH B 367
CRYST1 89.165 89.160 104.754 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 0.011215 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011216 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009546 0.00000
HETATM 1 N MSE A 1 41.505 24.789 55.962 1.00 33.04 N
HETATM 2 CA MSE A 1 41.342 26.276 55.904 1.00 32.22 C
HETATM 3 C MSE A 1 41.508 26.833 54.493 1.00 30.23 C
HETATM 4 O MSE A 1 42.406 26.442 53.746 1.00 29.58 O
HETATM 5 CB MSE A 1 42.299 26.973 56.884 1.00 32.33 C
HETATM 6 CG MSE A 1 41.904 28.409 57.216 1.00 33.37 C
HETATM 7 SE MSE A 1 42.913 29.219 58.705 0.85 37.00 SE
HETATM 8 CE MSE A 1 42.003 28.423 60.213 1.00 35.66 C
(ATOM LINES ARE NOT SHOWN.)
END
