HEADER LIGASE 24-MAR-00 1EOV
TITLE FREE ASPARTYL-TRNA SYNTHETASE (ASPRS) (E.C. 6.1.1.12) FROM YEAST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ENGINEERED ASPRS MONOMER LACKING THE 70 N-TERMINAL AMINO
COMPND 5 ACID RESIDUES;
COMPND 6 SYNONYM: ASPRS;
COMPND 7 EC: 6.1.1.12;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: APS GENE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TGE900;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTG908
KEYWDS AMINOACYL TRNA SYNTHETASE, TRNA LIGASE, APO-ENZYME, OB-FOLD, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SAUTER,B.LORBER,J.CAVARELLI,D.MORAS,R.GIEGE
REVDAT 5 09-AUG-23 1EOV 1 REMARK
REVDAT 4 13-JUL-11 1EOV 1 VERSN
REVDAT 3 24-FEB-09 1EOV 1 VERSN
REVDAT 2 01-APR-03 1EOV 1 JRNL
REVDAT 1 24-SEP-00 1EOV 0
JRNL AUTH C.SAUTER,B.LORBER,J.CAVARELLI,D.MORAS,R.GIEGE
JRNL TITL THE FREE YEAST ASPARTYL-TRNA SYNTHETASE DIFFERS FROM THE
JRNL TITL 2 TRNA(ASP)-COMPLEXED ENZYME BY STRUCTURAL CHANGES IN THE
JRNL TITL 3 CATALYTIC SITE, HINGE REGION, AND ANTICODON-BINDING DOMAIN.
JRNL REF J.MOL.BIOL. V. 299 1313 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10873455
JRNL DOI 10.1006/JMBI.2000.3791
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.SAUTER,B.LORBER,D.KERN,J.CAVARELLI,D.MORAS,R.GIEGE
REMARK 1 TITL CRYSTALLOGENESIS STUDIES ON YEAST ASPARTYL-TRNA SYNTHETASE:
REMARK 1 TITL 2 USE OF PHASE DIAGRAM TO IMPROVE CRYSTAL QUALITY.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 149 1999
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.CAVARELLI,G.ERIANI,B.REES,M.RUFF,M.BOEGLIN,A.MITSCHLER,
REMARK 1 AUTH 2 F.MARTIN,J.GANGLOFF,J.-C.THIERRY,D.MORAS
REMARK 1 TITL THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE:
REMARK 1 TITL 2 STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION
REMARK 1 TITL 3 REACTION.
REMARK 1 REF EMBO J. V. 13 327 1994
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.CAVARELLI,B.REES,M.RUFF,J.-C.THIERRY,D.MORAS
REMARK 1 TITL YEAST TRNA(ASP) RECOGNITION BY ITS COGNATE CLASS II
REMARK 1 TITL 2 AMINOACYL-TRNA SYNTHETASE.
REMARK 1 REF NATURE V. 362 181 1993
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/362181A0
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.RUFF,S.KRISHNASWAMY,M.BOEGLIN,A.POTERSZMAN,A.MITSCHLER,
REMARK 1 AUTH 2 A.PODJARNY,B.REES,J.-C.THIERRY,D.MORAS
REMARK 1 TITL CLASS II AMINOACYL TRANSFER RNA SYNTHETASES: CRYSTAL
REMARK 1 TITL 2 STRUCTURE OF YEAST ASPARTYL-TRNA SYNTHETASE COMPLEXED WITH
REMARK 1 TITL 3 TRNA(ASP).
REMARK 1 REF SCIENCE V. 252 1682 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 32837
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 SET) : 0.202
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2299
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.35
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1867
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 138
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3921
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 227
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.22000
REMARK 3 B22 (A**2) : 3.22000
REMARK 3 B33 (A**2) : -6.45000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.22
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.470
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.160
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 37.29
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MAXIMUM-LIKELYHOOD TARGET USING
REMARK 3 AMPLITUDES.
REMARK 4
REMARK 4 1EOV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010781.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-99
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.943
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34124
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1ASZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 MG/ML PROTEIN, 1.9 M AMMONIUM
REMARK 280 SULFATE, PH 5.60, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 278.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 92.45000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 45.11500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.22500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.11500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 45.11500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 138.67500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.11500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.11500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.22500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 45.11500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.11500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 138.67500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 92.45000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER CONSTRUCTED FROM
REMARK 300 CHAIN A AND A SYMMETRY PARTNER GENERATED BY THE TWO-FOLD.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
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 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 92.45000
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 LYS A 103 -8.91 -53.63
REMARK 500 ALA A 123 1.09 -162.49
REMARK 500 GLN A 133 -122.97 56.23
REMARK 500 SER A 150 175.26 -56.36
REMARK 500 PHE A 292 -129.55 58.10
REMARK 500 GLU A 315 -29.68 68.03
REMARK 500 ARG A 316 117.91 -161.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ASY RELATED DB: PDB
REMARK 900 1ASY CONTAINS THE SAME PROTEIN COMPLEXED WITH TRNAASP
REMARK 900 RELATED ID: 1ASZ RELATED DB: PDB
REMARK 900 1ASZ CONTAINS THE SAME PROTEIN COMPLEXED WITH TRNAASP AND ATP
DBREF 1EOV A 71 557 UNP P04802 SYDC_YEAST 70 556
SEQRES 1 A 487 ALA LYS ASP ASN TYR GLY LYS LEU PRO LEU ILE GLN SER
SEQRES 2 A 487 ARG ASP SER ASP ARG THR GLY GLN LYS ARG VAL LYS PHE
SEQRES 3 A 487 VAL ASP LEU ASP GLU ALA LYS ASP SER ASP LYS GLU VAL
SEQRES 4 A 487 LEU PHE ARG ALA ARG VAL HIS ASN THR ARG GLN GLN GLY
SEQRES 5 A 487 ALA THR LEU ALA PHE LEU THR LEU ARG GLN GLN ALA SER
SEQRES 6 A 487 LEU ILE GLN GLY LEU VAL LYS ALA ASN LYS GLU GLY THR
SEQRES 7 A 487 ILE SER LYS ASN MET VAL LYS TRP ALA GLY SER LEU ASN
SEQRES 8 A 487 LEU GLU SER ILE VAL LEU VAL ARG GLY ILE VAL LYS LYS
SEQRES 9 A 487 VAL ASP GLU PRO ILE LYS SER ALA THR VAL GLN ASN LEU
SEQRES 10 A 487 GLU ILE HIS ILE THR LYS ILE TYR THR ILE SER GLU THR
SEQRES 11 A 487 PRO GLU ALA LEU PRO ILE LEU LEU GLU ASP ALA SER ARG
SEQRES 12 A 487 SER GLU ALA GLU ALA GLU ALA ALA GLY LEU PRO VAL VAL
SEQRES 13 A 487 ASN LEU ASP THR ARG LEU ASP TYR ARG VAL ILE ASP LEU
SEQRES 14 A 487 ARG THR VAL THR ASN GLN ALA ILE PHE ARG ILE GLN ALA
SEQRES 15 A 487 GLY VAL CYS GLU LEU PHE ARG GLU TYR LEU ALA THR LYS
SEQRES 16 A 487 LYS PHE THR GLU VAL HIS THR PRO LYS LEU LEU GLY ALA
SEQRES 17 A 487 PRO SER GLU GLY GLY SER SER VAL PHE GLU VAL THR TYR
SEQRES 18 A 487 PHE LYS GLY LYS ALA TYR LEU ALA GLN SER PRO GLN PHE
SEQRES 19 A 487 ASN LYS GLN GLN LEU ILE VAL ALA ASP PHE GLU ARG VAL
SEQRES 20 A 487 TYR GLU ILE GLY PRO VAL PHE ARG ALA GLU ASN SER ASN
SEQRES 21 A 487 THR HIS ARG HIS MET THR GLU PHE THR GLY LEU ASP MET
SEQRES 22 A 487 GLU MET ALA PHE GLU GLU HIS TYR HIS GLU VAL LEU ASP
SEQRES 23 A 487 THR LEU SER GLU LEU PHE VAL PHE ILE PHE SER GLU LEU
SEQRES 24 A 487 PRO LYS ARG PHE ALA HIS GLU ILE GLU LEU VAL ARG LYS
SEQRES 25 A 487 GLN TYR PRO VAL GLU GLU PHE LYS LEU PRO LYS ASP GLY
SEQRES 26 A 487 LYS MET VAL ARG LEU THR TYR LYS GLU GLY ILE GLU MET
SEQRES 27 A 487 LEU ARG ALA ALA GLY LYS GLU ILE GLY ASP PHE GLU ASP
SEQRES 28 A 487 LEU SER THR GLU ASN GLU LYS PHE LEU GLY LYS LEU VAL
SEQRES 29 A 487 ARG ASP LYS TYR ASP THR ASP PHE TYR ILE LEU ASP LYS
SEQRES 30 A 487 PHE PRO LEU GLU ILE ARG PRO PHE TYR THR MET PRO ASP
SEQRES 31 A 487 PRO ALA ASN PRO LYS TYR SER ASN SER TYR ASP PHE PHE
SEQRES 32 A 487 MET ARG GLY GLU GLU ILE LEU SER GLY ALA GLN ARG ILE
SEQRES 33 A 487 HIS ASP HIS ALA LEU LEU GLN GLU ARG MET LYS ALA HIS
SEQRES 34 A 487 GLY LEU SER PRO GLU ASP PRO GLY LEU LYS ASP TYR CYS
SEQRES 35 A 487 ASP GLY PHE SER TYR GLY CYS PRO PRO HIS ALA GLY GLY
SEQRES 36 A 487 GLY ILE GLY LEU GLU ARG VAL VAL MET PHE TYR LEU ASP
SEQRES 37 A 487 LEU LYS ASN ILE ARG ARG ALA SER LEU PHE PRO ARG ASP
SEQRES 38 A 487 PRO LYS ARG LEU ARG PRO
FORMUL 2 HOH *227(H2 O)
HELIX 1 1 ARG A 84 ARG A 88 5 5
HELIX 2 2 LYS A 95 LEU A 99 5 5
HELIX 3 3 SER A 150 GLY A 158 1 9
HELIX 4 4 LEU A 207 SER A 212 1 6
HELIX 5 5 SER A 214 ALA A 221 1 8
HELIX 6 6 ASN A 227 TYR A 234 1 8
HELIX 7 7 TYR A 234 LEU A 239 1 6
HELIX 8 8 THR A 241 LYS A 265 1 25
HELIX 9 9 PRO A 302 ALA A 312 1 11
HELIX 10 10 TYR A 351 PHE A 373 1 23
HELIX 11 11 PHE A 373 TYR A 384 1 12
HELIX 12 12 TYR A 402 ALA A 412 1 11
HELIX 13 13 SER A 423 TYR A 438 1 16
HELIX 14 14 LEU A 450 ARG A 453 5 4
HELIX 15 15 ASP A 488 HIS A 499 1 12
HELIX 16 16 LEU A 508 SER A 516 1 9
HELIX 17 17 LEU A 529 LEU A 537 1 9
HELIX 18 18 ASN A 541 SER A 546 5 6
SHEET 1 A 7 TYR A 75 LYS A 77 0
SHEET 2 A 7 VAL A 184 SER A 198 1 O ILE A 194 N GLY A 76
SHEET 3 A 7 SER A 135 LYS A 142 1 O LEU A 136 N VAL A 184
SHEET 4 A 7 LEU A 125 GLN A 132 -1 O ALA A 126 N VAL A 141
SHEET 5 A 7 GLU A 108 GLN A 120 -1 O ARG A 114 N ARG A 131
SHEET 6 A 7 ILE A 165 LYS A 174 -1 N VAL A 166 O ALA A 113
SHEET 7 A 7 VAL A 184 SER A 198 -1 O GLU A 188 N LYS A 173
SHEET 1 B 3 LEU A 275 LEU A 276 0
SHEET 2 B 3 GLY A 294 LEU A 298 -1 O TYR A 297 N LEU A 276
SHEET 3 B 3 GLU A 288 TYR A 291 -1 N VAL A 289 O ALA A 296
SHEET 1 C 8 THR A 268 GLU A 269 0
SHEET 2 C 8 ARG A 316 PHE A 324 1 O ARG A 316 N THR A 268
SHEET 3 C 8 GLU A 337 ALA A 346 -1 O PHE A 338 N VAL A 323
SHEET 4 C 8 HIS A 522 GLY A 528 -1 O ALA A 523 N MET A 345
SHEET 5 C 8 GLU A 477 GLN A 484 -1 O SER A 481 N GLY A 526
SHEET 6 C 8 SER A 469 MET A 474 -1 N TYR A 470 O GLY A 482
SHEET 7 C 8 PHE A 442 ASP A 446 -1 O TYR A 443 N PHE A 473
SHEET 8 C 8 VAL A 398 THR A 401 1 O VAL A 398 N ILE A 444
CISPEP 1 ARG A 556 PRO A 557 0 -0.38
CRYST1 90.230 90.230 184.900 90.00 90.00 90.00 P 41 21 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 0.011083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005408 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
