HEADER HYDROLASE 30-SEP-06 2DZY
TITLE CRYSTAL STRUCTURE OF N392A MUTANT OF YEAST BLEOMYCIN HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE PROTEINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: Y3, BLEOMYCIN HYDROLASE, BLM HYDROLASE;
COMPND 5 EC: 3.4.22.40;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BLEOMYCIN HYDROLASE, THIOL PROTEASE, C1 PROTEASE, BURIED WATER,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.O'FARRELL,L.JOSHUA-TOR
REVDAT 5 25-OCT-23 2DZY 1 REMARK
REVDAT 4 10-NOV-21 2DZY 1 SEQADV
REVDAT 3 13-JUL-11 2DZY 1 VERSN
REVDAT 2 24-FEB-09 2DZY 1 VERSN
REVDAT 1 14-AUG-07 2DZY 0
JRNL AUTH P.A.O'FARRELL,L.JOSHUA-TOR
JRNL TITL MUTAGENESIS AND CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC
JRNL TITL 2 RESIDUES OF THE PAPAIN FAMILY PROTEASE BLEOMYCIN HYDROLASE:
JRNL TITL 3 NEW INSIGHTS INTO ACTIVE-SITE STRUCTURE
JRNL REF BIOCHEM.J. V. 401 421 2007
JRNL REFN ISSN 0264-6021
JRNL PMID 17007609
JRNL DOI 10.1042/BJ20060641
REMARK 2
REMARK 2 RESOLUTION. 2.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 242380.290
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 19270
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) : 0.198
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 940
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.57
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.73
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2885
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 178
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3686
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 187
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.78000
REMARK 3 B22 (A**2) : 0.78000
REMARK 3 B33 (A**2) : -1.56000
REMARK 3 B12 (A**2) : 4.75000
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) : 0.14
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.920
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.760 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.740 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.090 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.070 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 16.21
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.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DZY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000026052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19700
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.570
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1GCB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14-20% PEG 4K,100MM TRIS-HCL, PH 8.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.83450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.83450
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.83450
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 44.83450
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 44.83450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 44.83450
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 33750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 102770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 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 -0.500000 -0.866025 0.000000 151.02700
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 75.51350
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 130.79322
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 75.51350
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 130.79322
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 44.83450
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 151.02700
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 44.83450
REMARK 350 BIOMT1 6 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 44.83450
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 SER A 2 OG
REMARK 470 PHE A 17 CE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 93 CE NZ
REMARK 480 LYS A 309 CE NZ
REMARK 480 SER A 382 CB OG
REMARK 480 LYS A 383 CG CD CE NZ
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 68 -136.40 66.60
REMARK 500 LEU A 87 -71.64 -44.14
REMARK 500 ASN A 91 79.78 55.95
REMARK 500 ALA A 137 67.59 -152.60
REMARK 500 TYR A 163 91.07 -173.45
REMARK 500 ALA A 172 76.88 -163.93
REMARK 500 SER A 258 -60.02 -96.83
REMARK 500 PRO A 265 -7.42 -58.32
REMARK 500 PRO A 275 2.72 -59.77
REMARK 500 ARG A 287 -20.46 59.13
REMARK 500 ASN A 290 -49.88 -143.20
REMARK 500 ASN A 318 41.29 71.73
REMARK 500 PRO A 328 41.74 -104.12
REMARK 500 THR A 381 75.54 -52.42
REMARK 500 SER A 382 43.08 35.31
REMARK 500 LEU A 384 -169.22 -103.36
REMARK 500 SER A 393 55.65 -119.73
REMARK 500 PHE A 416 -48.76 -131.95
REMARK 500 SER A 435 -170.68 -65.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 33 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DZZ RELATED DB: PDB
REMARK 900 RELATED ID: 2E00 RELATED DB: PDB
REMARK 900 RELATED ID: 2E01 RELATED DB: PDB
REMARK 900 RELATED ID: 2E02 RELATED DB: PDB
REMARK 900 RELATED ID: 2E03 RELATED DB: PDB
DBREF 2DZY A 1 453 UNP Q01532 BLH1_YEAST 1 454
SEQADV 2DZY PHE A -3 UNP Q01532 EXPRESSION TAG
SEQADV 2DZY GLN A -2 UNP Q01532 EXPRESSION TAG
SEQADV 2DZY GLY A -1 UNP Q01532 EXPRESSION TAG
SEQADV 2DZY ALA A 0 UNP Q01532 EXPRESSION TAG
SEQADV 2DZY ALA A 392 UNP Q01532 ASN 392 ENGINEERED MUTATION
SEQADV 2DZY A UNP Q01532 LYS 454 DELETION
SEQRES 1 A 457 PHE GLN GLY ALA MET SER SER SER ILE ASP ILE SER LYS
SEQRES 2 A 457 ILE ASN SER TRP ASN LYS GLU PHE GLN SER ASP LEU THR
SEQRES 3 A 457 HIS GLN LEU ALA THR THR VAL LEU LYS ASN TYR ASN ALA
SEQRES 4 A 457 ASP ASP ALA LEU LEU ASN LYS THR ARG LEU GLN LYS GLN
SEQRES 5 A 457 ASP ASN ARG VAL PHE ASN THR VAL VAL SER THR ASP SER
SEQRES 6 A 457 THR PRO VAL THR ASN GLN LYS SER SER GLY ARG CYS TRP
SEQRES 7 A 457 LEU PHE ALA ALA THR ASN GLN LEU ARG LEU ASN VAL LEU
SEQRES 8 A 457 SER GLU LEU ASN LEU LYS GLU PHE GLU LEU SER GLN ALA
SEQRES 9 A 457 TYR LEU PHE PHE TYR ASP LYS LEU GLU LYS ALA ASN TYR
SEQRES 10 A 457 PHE LEU ASP GLN ILE VAL SER SER ALA ASP GLN ASP ILE
SEQRES 11 A 457 ASP SER ARG LEU VAL GLN TYR LEU LEU ALA ALA PRO THR
SEQRES 12 A 457 GLU ASP GLY GLY GLN TYR SER MET PHE LEU ASN LEU VAL
SEQRES 13 A 457 LYS LYS TYR GLY LEU ILE PRO LYS ASP LEU TYR GLY ASP
SEQRES 14 A 457 LEU PRO TYR SER THR THR ALA SER ARG LYS TRP ASN SER
SEQRES 15 A 457 LEU LEU THR THR LYS LEU ARG GLU PHE ALA GLU THR LEU
SEQRES 16 A 457 ARG THR ALA LEU LYS GLU ARG SER ALA ASP ASP SER ILE
SEQRES 17 A 457 ILE VAL THR LEU ARG GLU GLN MET GLN ARG GLU ILE PHE
SEQRES 18 A 457 ARG LEU MET SER LEU PHE MET ASP ILE PRO PRO VAL GLN
SEQRES 19 A 457 PRO ASN GLU GLN PHE THR TRP GLU TYR VAL ASP LYS ASP
SEQRES 20 A 457 LYS LYS ILE HIS THR ILE LYS SER THR PRO LEU GLU PHE
SEQRES 21 A 457 ALA SER LYS TYR ALA LYS LEU ASP PRO SER THR PRO VAL
SEQRES 22 A 457 SER LEU ILE ASN ASP PRO ARG HIS PRO TYR GLY LYS LEU
SEQRES 23 A 457 ILE LYS ILE ASP ARG LEU GLY ASN VAL LEU GLY GLY ASP
SEQRES 24 A 457 ALA VAL ILE TYR LEU ASN VAL ASP ASN GLU THR LEU SER
SEQRES 25 A 457 LYS LEU VAL VAL LYS ARG LEU GLN ASN ASN LYS ALA VAL
SEQRES 26 A 457 PHE PHE GLY SER HIS THR PRO LYS PHE MET ASP LYS LYS
SEQRES 27 A 457 THR GLY VAL MET ASP ILE GLU LEU TRP ASN TYR PRO ALA
SEQRES 28 A 457 ILE GLY TYR ASN LEU PRO GLN GLN LYS ALA SER ARG ILE
SEQRES 29 A 457 ARG TYR HIS GLU SER LEU MET THR HIS ALA MET LEU ILE
SEQRES 30 A 457 THR GLY CYS HIS VAL ASP GLU THR SER LYS LEU PRO LEU
SEQRES 31 A 457 ARG TYR ARG VAL GLU ALA SER TRP GLY LYS ASP SER GLY
SEQRES 32 A 457 LYS ASP GLY LEU TYR VAL MET THR GLN LYS TYR PHE GLU
SEQRES 33 A 457 GLU TYR CYS PHE GLN ILE VAL VAL ASP ILE ASN GLU LEU
SEQRES 34 A 457 PRO LYS GLU LEU ALA SER LYS PHE THR SER GLY LYS GLU
SEQRES 35 A 457 GLU PRO ILE VAL LEU PRO ILE TRP ASP PRO MET GLY ALA
SEQRES 36 A 457 LEU ALA
FORMUL 2 HOH *187(H2 O)
HELIX 1 1 PHE A -3 SER A 4 1 8
HELIX 2 2 ASP A 6 SER A 19 1 14
HELIX 3 3 ASP A 20 TYR A 33 1 14
HELIX 4 4 ASN A 34 LEU A 40 1 7
HELIX 5 5 ASN A 41 ASP A 49 1 9
HELIX 6 6 ARG A 72 ASN A 91 1 20
HELIX 7 7 SER A 98 SER A 121 1 24
HELIX 8 8 SER A 128 ALA A 137 1 10
HELIX 9 9 GLN A 144 GLY A 156 1 13
HELIX 10 10 PRO A 159 TYR A 163 5 5
HELIX 11 11 PRO A 167 THR A 171 5 5
HELIX 12 12 SER A 173 ARG A 198 1 26
HELIX 13 13 ASP A 202 MET A 224 1 23
HELIX 14 14 THR A 252 TYR A 260 1 9
HELIX 15 15 ASP A 303 ASN A 317 1 15
HELIX 16 16 ASN A 344 GLY A 349 5 6
HELIX 17 17 GLN A 355 TYR A 362 1 8
HELIX 18 18 GLN A 408 TYR A 414 1 7
HELIX 19 19 ASN A 423 LEU A 425 5 3
HELIX 20 20 PRO A 426 SER A 435 1 10
SHEET 1 A 6 THR A 55 VAL A 56 0
SHEET 2 A 6 HIS A 369 VAL A 378 -1 O CYS A 376 N THR A 55
SHEET 3 A 6 PRO A 385 GLU A 391 -1 O GLU A 391 N LEU A 372
SHEET 4 A 6 LEU A 403 THR A 407 -1 O TYR A 404 N VAL A 390
SHEET 5 A 6 VAL A 337 MET A 338 1 N MET A 338 O VAL A 405
SHEET 6 A 6 MET A 331 ASP A 332 -1 N ASP A 332 O VAL A 337
SHEET 1 B 8 THR A 55 VAL A 56 0
SHEET 2 B 8 HIS A 369 VAL A 378 -1 O CYS A 376 N THR A 55
SHEET 3 B 8 VAL A 321 SER A 325 -1 N VAL A 321 O ILE A 373
SHEET 4 B 8 CYS A 415 ASP A 421 -1 O PHE A 416 N GLY A 324
SHEET 5 B 8 PRO A 268 ILE A 272 -1 N VAL A 269 O VAL A 420
SHEET 6 B 8 VAL A 297 ASN A 301 1 O LEU A 300 N ILE A 272
SHEET 7 B 8 LEU A 282 ILE A 285 -1 N ILE A 283 O TYR A 299
SHEET 8 B 8 ILE A 441 LEU A 443 1 O ILE A 441 N LEU A 282
SHEET 1 C 2 PHE A 235 VAL A 240 0
SHEET 2 C 2 ILE A 246 SER A 251 -1 O SER A 251 N PHE A 235
CISPEP 1 THR A 62 PRO A 63 0 0.03
CISPEP 2 THR A 327 PRO A 328 0 -0.58
CRYST1 151.027 151.027 89.669 90.00 90.00 120.00 P 63 2 2 12
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 0.006621 0.003823 0.000000 0.00000
SCALE2 0.000000 0.007646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011152 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
