HEADER LIGASE 27-JAN-10 3LK7
TITLE THE CRYSTAL STRUCTURE OF UDP-N-ACETYLMURAMOYLALANINE-D-GLUTAMATE
TITLE 2 (MURD) LIGASE FROM STREPTOCOCCUS AGALACTIAE TO 1.5A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE SYNTHETASE, D-
COMPND 5 GLUTAMIC ACID-ADDING ENZYME;
COMPND 6 EC: 6.3.2.9;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE;
SOURCE 3 ORGANISM_TAXID: 216466;
SOURCE 4 STRAIN: 2603V, SEROGROUP V;
SOURCE 5 GENE: MURD, SAG0475;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS UDP-N-ACETYLMURAMOYLALANINE, D-GLUTAMATE, STREPTOCOCCUS, AGALACITAE,
KEYWDS 2 PSI, MCSG, STRUCTURAL GENOMICS, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, PROTEIN STRUCTURE INITIATIVE, ATP-BINDING, CELL CYCLE,
KEYWDS 4 CELL DIVISION, CELL SHAPE, CELL WALL BIOGENESIS/DEGRADATION,
KEYWDS 5 CYTOPLASM, NUCLEOTIDE-BINDING, PEPTIDOGLYCAN SYNTHESIS, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.STEIN,A.SATHER,G.SHAKELFORD,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 2 01-NOV-17 3LK7 1 REMARK
REVDAT 1 09-FEB-10 3LK7 0
JRNL AUTH A.J.STEIN,A.SATHER,G.SHAKELFORD,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF
JRNL TITL 2 UDP-N-ACETYLMURAMOYLALANINE-D-GLUTAMATE (MURD) LIGASE FROM
JRNL TITL 3 STREPTOCOCCUS AGALACTIAE TO 1.5A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.5.0102
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 82903
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4139
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5468
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 263
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 401
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.72000
REMARK 3 B22 (A**2) : 2.27000
REMARK 3 B33 (A**2) : -1.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.74000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.070
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.286
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
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): 3515 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4788 ; 1.342 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 474 ; 5.965 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;36.790 ;25.556
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 610 ;11.707 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;11.175 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 566 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2616 ; 0.007 ; 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): 2258 ; 0.801 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3644 ; 1.427 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1257 ; 2.477 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1130 ; 3.846 ; 4.500
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 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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3LK7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057378.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-09
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83028
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SHELX, MLPHARE, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.1M TRIS PH 8.5, 0.2M
REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 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 80.76950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.52250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.76950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.52250
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 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 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 LYS A 2
REMARK 465 THR A 3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 10 CG CD CE NZ
REMARK 470 GLU A 54 CG CD OE1 OE2
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 GLN A 113 CG CD OE1 NE2
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 GLU A 364 CG CD OE1 OE2
REMARK 470 GLN A 390 CG CD OE1 NE2
REMARK 470 GLU A 451 CG CD OE1 OE2
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 O HOH A 809 O HOH A 810 2.06
REMARK 500 NZ LYS A 207 O HOH A 810 2.12
REMARK 500 NZ LYS A 207 O HOH A 809 2.16
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 LEU A 17 -83.70 -110.29
REMARK 500 ALA A 18 -138.46 53.26
REMARK 500 ASN A 159 -169.33 -129.10
REMARK 500 LYS A 177 -62.47 -138.65
REMARK 500 PHE A 179 119.60 -36.27
REMARK 500 HIS A 312 -2.46 75.66
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 452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 454
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC89407 RELATED DB: TARGETDB
DBREF 3LK7 A 1 451 UNP Q8E186 MURD_STRA5 1 451
SEQRES 1 A 451 MSE LYS THR ILE THR THR PHE GLU ASN LYS LYS VAL LEU
SEQRES 2 A 451 VAL LEU GLY LEU ALA ARG SER GLY GLU ALA ALA ALA ARG
SEQRES 3 A 451 LEU LEU ALA LYS LEU GLY ALA ILE VAL THR VAL ASN ASP
SEQRES 4 A 451 GLY LYS PRO PHE ASP GLU ASN PRO THR ALA GLN SER LEU
SEQRES 5 A 451 LEU GLU GLU GLY ILE LYS VAL VAL CYS GLY SER HIS PRO
SEQRES 6 A 451 LEU GLU LEU LEU ASP GLU ASP PHE CYS TYR MSE ILE LYS
SEQRES 7 A 451 ASN PRO GLY ILE PRO TYR ASN ASN PRO MSE VAL LYS LYS
SEQRES 8 A 451 ALA LEU GLU LYS GLN ILE PRO VAL LEU THR GLU VAL GLU
SEQRES 9 A 451 LEU ALA TYR LEU VAL SER GLU SER GLN LEU ILE GLY ILE
SEQRES 10 A 451 THR GLY SER ASN GLY LYS THR THR THR THR THR MSE ILE
SEQRES 11 A 451 ALA GLU VAL LEU ASN ALA GLY GLY GLN ARG GLY LEU LEU
SEQRES 12 A 451 ALA GLY ASN ILE GLY PHE PRO ALA SER GLU VAL VAL GLN
SEQRES 13 A 451 ALA ALA ASN ASP LYS ASP THR LEU VAL MSE GLU LEU SER
SEQRES 14 A 451 SER PHE GLN LEU MSE GLY VAL LYS GLU PHE ARG PRO HIS
SEQRES 15 A 451 ILE ALA VAL ILE THR ASN LEU MSE PRO THR HIS LEU ASP
SEQRES 16 A 451 TYR HIS GLY SER PHE GLU ASP TYR VAL ALA ALA LYS TRP
SEQRES 17 A 451 ASN ILE GLN ASN GLN MSE SER SER SER ASP PHE LEU VAL
SEQRES 18 A 451 LEU ASN PHE ASN GLN GLY ILE SER LYS GLU LEU ALA LYS
SEQRES 19 A 451 THR THR LYS ALA THR ILE VAL PRO PHE SER THR THR GLU
SEQRES 20 A 451 LYS VAL ASP GLY ALA TYR VAL GLN ASP LYS GLN LEU PHE
SEQRES 21 A 451 TYR LYS GLY GLU ASN ILE MSE SER VAL ASP ASP ILE GLY
SEQRES 22 A 451 VAL PRO GLY SER HIS ASN VAL GLU ASN ALA LEU ALA THR
SEQRES 23 A 451 ILE ALA VAL ALA LYS LEU ALA GLY ILE SER ASN GLN VAL
SEQRES 24 A 451 ILE ARG GLU THR LEU SER ASN PHE GLY GLY VAL LYS HIS
SEQRES 25 A 451 ARG LEU GLN SER LEU GLY LYS VAL HIS GLY ILE SER PHE
SEQRES 26 A 451 TYR ASN ASP SER LYS SER THR ASN ILE LEU ALA THR GLN
SEQRES 27 A 451 LYS ALA LEU SER GLY PHE ASP ASN THR LYS VAL ILE LEU
SEQRES 28 A 451 ILE ALA GLY GLY LEU ASP ARG GLY ASN GLU PHE ASP GLU
SEQRES 29 A 451 LEU ILE PRO ASP ILE THR GLY LEU LYS HIS MSE VAL VAL
SEQRES 30 A 451 LEU GLY GLU SER ALA SER ARG VAL LYS ARG ALA ALA GLN
SEQRES 31 A 451 LYS ALA GLY VAL THR TYR SER ASP ALA LEU ASP VAL ARG
SEQRES 32 A 451 ASP ALA VAL HIS LYS ALA TYR GLU VAL ALA GLN GLN GLY
SEQRES 33 A 451 ASP VAL ILE LEU LEU SER PRO ALA ASN ALA SER TRP ASP
SEQRES 34 A 451 MSE TYR LYS ASN PHE GLU VAL ARG GLY ASP GLU PHE ILE
SEQRES 35 A 451 ASP THR PHE GLU SER LEU ARG GLY GLU
MODRES 3LK7 MSE A 76 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 88 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 129 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 166 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 174 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 190 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 214 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 267 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 375 MET SELENOMETHIONINE
MODRES 3LK7 MSE A 430 MET SELENOMETHIONINE
HET MSE A 76 8
HET MSE A 88 8
HET MSE A 129 8
HET MSE A 166 8
HET MSE A 174 8
HET MSE A 190 8
HET MSE A 214 8
HET MSE A 267 8
HET MSE A 375 13
HET MSE A 430 8
HET SO4 A 452 5
HET SO4 A 453 5
HET CL A 454 1
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 CL CL 1-
FORMUL 5 HOH *401(H2 O)
HELIX 1 1 SER A 20 LEU A 31 1 12
HELIX 2 2 PRO A 42 GLU A 45 5 4
HELIX 3 3 ASN A 46 GLU A 55 1 10
HELIX 4 4 PRO A 65 GLU A 71 5 7
HELIX 5 5 ASN A 86 LYS A 95 1 10
HELIX 6 6 THR A 101 SER A 110 1 10
HELIX 7 7 GLY A 122 GLY A 137 1 16
HELIX 8 8 PRO A 150 VAL A 155 1 6
HELIX 9 9 SER A 169 MSE A 174 1 6
HELIX 10 10 HIS A 193 GLY A 198 1 6
HELIX 11 11 SER A 199 ASN A 209 1 11
HELIX 12 12 ILE A 210 ASN A 212 5 3
HELIX 13 13 GLN A 226 LYS A 234 1 9
HELIX 14 14 ASP A 270 ILE A 272 5 3
HELIX 15 15 GLY A 276 GLY A 294 1 19
HELIX 16 16 SER A 296 PHE A 307 1 12
HELIX 17 17 ASN A 333 GLY A 343 1 11
HELIX 18 18 PHE A 344 THR A 347 5 4
HELIX 19 19 PHE A 362 GLU A 364 5 3
HELIX 20 20 LEU A 365 THR A 370 1 6
HELIX 21 21 SER A 381 ALA A 392 1 12
HELIX 22 22 ASP A 401 ALA A 413 1 13
HELIX 23 23 ASN A 433 GLY A 450 1 18
SHEET 1 A 5 LYS A 58 CYS A 61 0
SHEET 2 A 5 ILE A 34 ASP A 39 1 N VAL A 37 O LYS A 58
SHEET 3 A 5 LYS A 11 LEU A 15 1 N VAL A 14 O THR A 36
SHEET 4 A 5 PHE A 73 LYS A 78 1 O CYS A 74 N LYS A 11
SHEET 5 A 5 VAL A 99 LEU A 100 1 O LEU A 100 N MSE A 76
SHEET 1 B 9 GLY A 141 GLY A 145 0
SHEET 2 B 9 THR A 163 GLU A 167 1 O THR A 163 N LEU A 142
SHEET 3 B 9 GLN A 113 THR A 118 1 N GLN A 113 O LEU A 164
SHEET 4 B 9 ILE A 183 ILE A 186 1 O VAL A 185 N THR A 118
SHEET 5 B 9 PHE A 219 ASN A 223 1 O VAL A 221 N ALA A 184
SHEET 6 B 9 THR A 239 SER A 244 1 O VAL A 241 N LEU A 220
SHEET 7 B 9 ALA A 252 GLN A 255 1 O ALA A 252 N PRO A 242
SHEET 8 B 9 GLN A 258 TYR A 261 -1 O PHE A 260 N TYR A 253
SHEET 9 B 9 GLU A 264 SER A 268 -1 O MSE A 267 N LEU A 259
SHEET 1 C 6 GLN A 315 VAL A 320 0
SHEET 2 C 6 ILE A 323 ASN A 327 -1 O PHE A 325 N LEU A 317
SHEET 3 C 6 VAL A 418 LEU A 421 1 O ILE A 419 N SER A 324
SHEET 4 C 6 VAL A 349 ALA A 353 1 N ILE A 352 O LEU A 420
SHEET 5 C 6 HIS A 374 VAL A 377 1 O VAL A 376 N LEU A 351
SHEET 6 C 6 TYR A 396 ASP A 398 1 O SER A 397 N VAL A 377
LINK C TYR A 75 N MSE A 76 1555 1555 1.34
LINK C MSE A 76 N ILE A 77 1555 1555 1.33
LINK C PRO A 87 N MSE A 88 1555 1555 1.34
LINK C MSE A 88 N VAL A 89 1555 1555 1.33
LINK C THR A 128 N MSE A 129 1555 1555 1.33
LINK C MSE A 129 N ILE A 130 1555 1555 1.33
LINK C VAL A 165 N MSE A 166 1555 1555 1.33
LINK C MSE A 166 N GLU A 167 1555 1555 1.34
LINK C LEU A 173 N MSE A 174 1555 1555 1.34
LINK C MSE A 174 N GLY A 175 1555 1555 1.33
LINK C LEU A 189 N MSE A 190 1555 1555 1.32
LINK C MSE A 190 N PRO A 191 1555 1555 1.34
LINK C GLN A 213 N MSE A 214 1555 1555 1.33
LINK C MSE A 214 N SER A 215 1555 1555 1.34
LINK C ILE A 266 N MSE A 267 1555 1555 1.33
LINK C MSE A 267 N SER A 268 1555 1555 1.33
LINK C HIS A 374 N MSE A 375 1555 1555 1.33
LINK C MSE A 375 N VAL A 376 1555 1555 1.32
LINK C ASP A 429 N MSE A 430 1555 1555 1.34
LINK C MSE A 430 N TYR A 431 1555 1555 1.34
SITE 1 AC1 10 ASN A 121 GLY A 122 LYS A 123 THR A 124
SITE 2 AC1 10 HOH A 458 HOH A 521 HOH A 549 HOH A 626
SITE 3 AC1 10 HOH A 694 HOH A 829
SITE 1 AC2 10 GLY A 40 HIS A 64 SER A 296 ASN A 297
SITE 2 AC2 10 GLN A 298 HOH A 540 HOH A 717 HOH A 734
SITE 3 AC2 10 HOH A 751 HOH A 778
SITE 1 AC3 4 ARG A 19 TRP A 428 ASN A 433 PHE A 434
CRYST1 161.539 65.045 52.889 90.00 107.52 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 0.006190 0.000000 0.001954 0.00000
SCALE2 0.000000 0.015374 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019827 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
