HEADER LYASE 09-MAR-11 3R0Z
TITLE CRYSTAL STRUCTURE OF APO D-SERINE DEAMINASE FROM SALMONELLA
TITLE 2 TYPHIMURIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-SERINE DEHYDRATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: D-SERINE DEAMINASE, DSD;
COMPND 5 EC: 4.3.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 3 TYPHIMURIUM;
SOURCE 4 ORGANISM_TAXID: 90371;
SOURCE 5 GENE: DSDA, STM3802;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B(+)
KEYWDS FOLDTYPE 2 FAMILY OF PLP-DEPENDENT ENZYMES, ALPHA, BETA ELIMINATION
KEYWDS 2 OF D-SERINE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.R.BHARATH,B.SHVETA,H.S.SAVITHRI,M.R.N.MURTHY
REVDAT 2 20-MAR-24 3R0Z 1 REMARK SEQADV
REVDAT 1 29-JUN-11 3R0Z 0
JRNL AUTH S.R.BHARATH,S.BISHT,H.S.SAVITHRI,M.R.N.MURTHY
JRNL TITL CRYSTAL STRUCTURES OF OPEN AND CLOSED FORMS OF D-SERINE
JRNL TITL 2 DEAMINASE FROM SALMONELLA TYPHIMURIUM - IMPLICATIONS ON
JRNL TITL 3 SUBSTRATE SPECIFICITY AND CATALYSIS
JRNL REF FEBS J. 2011
JRNL REFN ISSN 1742-464X
JRNL PMID 21668644
JRNL DOI 10.1111/J.1742-4658.2011.08210.X
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 16864
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 910
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1071
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 68
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3220
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.02000
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): 0.302
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.232
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.895
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3318 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4498 ; 1.437 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 434 ; 6.290 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;33.740 ;24.234
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 515 ;17.077 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;20.456 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 500 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2517 ; 0.006 ; 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): 2136 ; 0.660 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3375 ; 1.162 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1182 ; 1.861 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1121 ; 2.815 ; 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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 3R0Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064352.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17806
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 49.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.49200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE PH 6.1, 0.4M
REMARK 280 AMMONIUM SULPHATE, 0.8M AMMONIUM SULPHATE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
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 50.01000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.39500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.01000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.39500
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 ALA A 69
REMARK 465 ALA A 70
REMARK 465 ALA A 71
REMARK 465 ASP A 235
REMARK 465 ASP A 236
REMARK 465 GLU A 237
REMARK 465 ASN A 238
REMARK 465 LEU A 441
REMARK 465 GLU A 442
REMARK 465 HIS A 443
REMARK 465 HIS A 444
REMARK 465 HIS A 445
REMARK 465 HIS A 446
REMARK 465 HIS A 447
REMARK 465 HIS A 448
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 MET A 1 CG SD CE
REMARK 470 GLU A 2 CG CD OE1 OE2
REMARK 470 ASN A 3 CG OD1 ND2
REMARK 470 LYS A 6 CE NZ
REMARK 470 ARG A 10 CG CD NE CZ NH1 NH2
REMARK 470 THR A 68 OG1 CG2
REMARK 470 LYS A 183 NZ
REMARK 470 LYS A 197 CE NZ
REMARK 470 LYS A 199 CG CD CE NZ
REMARK 470 ASP A 212 CG OD1 OD2
REMARK 470 ASP A 213 CG OD1 OD2
REMARK 470 TYR A 214 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 216 CG1 CG2
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 GLN A 220 CG CD OE1 NE2
REMARK 470 ARG A 240 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 440 CG CD NE CZ NH1 NH2
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 ASN A 3 15.73 -59.69
REMARK 500 ALA A 19 2.76 -67.44
REMARK 500 ARG A 56 -37.38 -37.74
REMARK 500 LYS A 105 54.92 -96.48
REMARK 500 ILE A 111 -63.48 72.88
REMARK 500 SER A 307 58.21 -150.12
REMARK 500 HIS A 319 -115.38 67.76
REMARK 500 ALA A 437 39.67 -83.42
REMARK 500 LYS A 438 44.62 -155.51
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 449
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 453
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R0X RELATED DB: PDB
DBREF 3R0Z A 1 440 UNP Q8ZL08 SDHD_SALTY 1 440
SEQADV 3R0Z LEU A 441 UNP Q8ZL08 EXPRESSION TAG
SEQADV 3R0Z GLU A 442 UNP Q8ZL08 EXPRESSION TAG
SEQADV 3R0Z HIS A 443 UNP Q8ZL08 EXPRESSION TAG
SEQADV 3R0Z HIS A 444 UNP Q8ZL08 EXPRESSION TAG
SEQADV 3R0Z HIS A 445 UNP Q8ZL08 EXPRESSION TAG
SEQADV 3R0Z HIS A 446 UNP Q8ZL08 EXPRESSION TAG
SEQADV 3R0Z HIS A 447 UNP Q8ZL08 EXPRESSION TAG
SEQADV 3R0Z HIS A 448 UNP Q8ZL08 EXPRESSION TAG
SEQRES 1 A 448 MET GLU ASN ILE GLN LYS LEU ILE ALA ARG TYR PRO LEU
SEQRES 2 A 448 VAL GLU ASP LEU VAL ALA LEU LYS GLU THR THR TRP PHE
SEQRES 3 A 448 ASN PRO GLY ALA THR SER LEU ALA GLN GLY LEU PRO TYR
SEQRES 4 A 448 VAL GLY LEU THR GLU GLN ASP VAL ASN ALA ALA HIS ASP
SEQRES 5 A 448 ARG LEU ALA ARG PHE ALA PRO TYR LEU ALA LYS ALA PHE
SEQRES 6 A 448 PRO GLN THR ALA ALA ALA GLY GLY MET ILE GLU SER ASP
SEQRES 7 A 448 VAL VAL ALA ILE PRO ALA MET GLN LYS ARG LEU GLU LYS
SEQRES 8 A 448 GLU TYR GLY GLN THR ILE ASN GLY GLU MET LEU LEU LYS
SEQRES 9 A 448 LYS ASP SER HIS LEU ALA ILE SER GLY SER ILE LYS ALA
SEQRES 10 A 448 ARG GLY GLY ILE TYR GLU VAL LEU THR HIS ALA GLU LYS
SEQRES 11 A 448 LEU ALA LEU GLU ALA GLY LEU LEU THR THR ASP ASP ASP
SEQRES 12 A 448 TYR SER VAL LEU LEU SER PRO GLU PHE LYS GLN PHE PHE
SEQRES 13 A 448 SER GLN TYR SER ILE ALA VAL GLY SER THR GLY ASN LEU
SEQRES 14 A 448 GLY LEU SER ILE GLY ILE MET SER ALA CYS ILE GLY PHE
SEQRES 15 A 448 LYS VAL THR VAL HIS MET SER ALA ASP ALA ARG ALA TRP
SEQRES 16 A 448 LYS LYS ALA LYS LEU ARG SER HIS GLY VAL THR VAL VAL
SEQRES 17 A 448 GLU TYR GLU ASP ASP TYR GLY VAL ALA VAL GLU GLN GLY
SEQRES 18 A 448 ARG LYS ALA ALA GLN SER ASP PRO ASN CYS PHE PHE ILE
SEQRES 19 A 448 ASP ASP GLU ASN SER ARG THR LEU PHE LEU GLY TYR ALA
SEQRES 20 A 448 VAL ALA GLY GLN ARG LEU LYS ALA GLN PHE ALA GLN GLN
SEQRES 21 A 448 GLY ARG VAL VAL ASP ALA SER HIS PRO LEU PHE VAL TYR
SEQRES 22 A 448 LEU PRO CYS GLY VAL GLY GLY GLY PRO GLY GLY VAL ALA
SEQRES 23 A 448 PHE GLY LEU LYS LEU ALA PHE GLY ASP ASN VAL HIS CYS
SEQRES 24 A 448 PHE PHE ALA GLU PRO THR HIS SER PRO CYS MET LEU LEU
SEQRES 25 A 448 GLY VAL TYR THR GLY LEU HIS ASP ALA ILE SER VAL GLN
SEQRES 26 A 448 ASP ILE GLY ILE ASP ASN LEU THR ALA ALA ASP GLY LEU
SEQRES 27 A 448 ALA VAL GLY ARG ALA SER GLY PHE VAL GLY ARG ALA MET
SEQRES 28 A 448 GLU ARG LEU LEU ASP GLY LEU TYR THR LEU ASP ASP GLN
SEQRES 29 A 448 THR MET TYR ASP MET LEU GLY TRP LEU ALA GLN GLU GLU
SEQRES 30 A 448 GLY ILE ARG LEU GLU PRO SER ALA LEU ALA GLY MET ALA
SEQRES 31 A 448 GLY PRO GLN ARG ILE CYS ALA SER VAL ALA TYR GLN GLN
SEQRES 32 A 448 ARG HIS GLY PHE SER GLN THR GLN LEU GLY ASN ALA THR
SEQRES 33 A 448 HIS LEU VAL TRP ALA THR GLY GLY GLY MET VAL PRO GLU
SEQRES 34 A 448 ASP GLU MET GLU GLN TYR LEU ALA LYS GLY ARG LEU GLU
SEQRES 35 A 448 HIS HIS HIS HIS HIS HIS
HET SO4 A 449 5
HET SO4 A 450 5
HET SO4 A 451 5
HET EDO A 452 4
HET EDO A 453 4
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 7 HOH *140(H2 O)
HELIX 1 1 ASN A 3 TYR A 11 1 9
HELIX 2 2 LEU A 13 ALA A 19 1 7
HELIX 3 3 SER A 32 LEU A 37 1 6
HELIX 4 4 PRO A 38 VAL A 40 5 3
HELIX 5 5 THR A 43 PHE A 65 1 23
HELIX 6 6 ILE A 82 GLY A 94 1 13
HELIX 7 7 SER A 107 LEU A 109 5 3
HELIX 8 8 ILE A 115 ALA A 135 1 21
HELIX 9 9 ASP A 143 LEU A 148 5 6
HELIX 10 10 SER A 149 SER A 157 1 9
HELIX 11 11 GLY A 167 GLY A 181 1 15
HELIX 12 12 ARG A 193 HIS A 203 1 11
HELIX 13 13 GLY A 215 SER A 227 1 13
HELIX 14 14 SER A 239 VAL A 248 1 10
HELIX 15 15 VAL A 248 GLY A 261 1 14
HELIX 16 16 GLY A 279 GLY A 294 1 16
HELIX 17 17 PRO A 308 GLY A 317 1 10
HELIX 18 18 LEU A 318 ILE A 322 5 5
HELIX 19 19 ALA A 335 ALA A 339 5 5
HELIX 20 20 SER A 344 GLU A 352 1 9
HELIX 21 21 ARG A 353 LEU A 355 5 3
HELIX 22 22 ASP A 362 GLY A 378 1 17
HELIX 23 23 GLU A 382 MET A 389 5 8
HELIX 24 24 ALA A 390 SER A 398 1 9
HELIX 25 25 SER A 398 HIS A 405 1 8
HELIX 26 26 SER A 408 ASN A 414 1 7
HELIX 27 27 PRO A 428 ALA A 437 1 10
SHEET 1 A 7 THR A 24 PHE A 26 0
SHEET 2 A 7 GLY A 357 LEU A 361 -1 O LEU A 358 N TRP A 25
SHEET 3 A 7 VAL A 297 PRO A 304 1 N PHE A 301 O TYR A 359
SHEET 4 A 7 LEU A 270 PRO A 275 1 N LEU A 270 O HIS A 298
SHEET 5 A 7 THR A 416 ALA A 421 1 O LEU A 418 N PHE A 271
SHEET 6 A 7 GLU A 100 LYS A 105 1 N LEU A 102 O HIS A 417
SHEET 7 A 7 VAL A 79 ALA A 81 -1 N VAL A 80 O LEU A 103
SHEET 1 B 4 THR A 206 TYR A 210 0
SHEET 2 B 4 LYS A 183 SER A 189 1 N MET A 188 O VAL A 208
SHEET 3 B 4 SER A 160 GLY A 164 1 N VAL A 163 O HIS A 187
SHEET 4 B 4 CYS A 231 PHE A 233 1 O PHE A 232 N ALA A 162
SITE 1 AC1 8 LYS A 116 GLY A 277 VAL A 278 GLY A 279
SITE 2 AC1 8 GLY A 280 GLY A 281 PRO A 282 HOH A 499
SITE 1 AC2 4 SER A 344 GLY A 345 PHE A 346 HOH A 474
SITE 1 AC3 8 LYS A 116 GLY A 167 ASN A 168 GLY A 337
SITE 2 AC3 8 HOH A 455 HOH A 473 HOH A 499 HOH A 588
SITE 1 AC4 4 LYS A 105 HIS A 108 GLY A 378 ARG A 380
SITE 1 AC5 3 SER A 239 ARG A 240 THR A 241
CRYST1 100.020 46.790 100.040 90.00 93.75 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 0.009998 0.000000 0.000655 0.00000
SCALE2 0.000000 0.021372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010017 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
