HEADER DNA BINDING PROTEIN 18-JUL-95 1GCB
TITLE GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAL6 HG (EMTS) DERIVATIVE;
COMPND 3 CHAIN: A;
COMPND 4 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 STRAIN: SC277;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS DNA-BINDING, PEPTIDASE, CYSTEINE PROTEASE, REGULATORY FACTOR,
KEYWDS 2 BLEOMYCIN HYDROLASE, RING PROTEIN, DNA-BINDING PROTEIN, DNA BINDING
KEYWDS 3 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.JOSHUA-TOR,H.E.XU,S.A.JOHNSTON,D.C.REES
REVDAT 4 07-FEB-24 1GCB 1 KEYWDS REMARK LINK
REVDAT 3 13-JUL-11 1GCB 1 VERSN
REVDAT 2 24-FEB-09 1GCB 1 VERSN
REVDAT 1 15-OCT-95 1GCB 0
JRNL AUTH L.JOSHUA-TOR,H.E.XU,S.A.JOHNSTON,D.C.REES
JRNL TITL CRYSTAL STRUCTURE OF A CONSERVED PROTEASE THAT BINDS DNA:
JRNL TITL 2 THE BLEOMYCIN HYDROLASE, GAL6.
JRNL REF SCIENCE V. 269 945 1995
JRNL REFN ISSN 0036-8075
JRNL PMID 7638617
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.E.XU,S.A.JOHNSTON
REMARK 1 TITL YEAST BLEOMYCIN HYDROLASE IS A DNA-BINDING CYSTEINE
REMARK 1 TITL 2 PROTEASE: IDENTIFICATION, PURIFICATION, BIOCHEMICAL
REMARK 1 TITL 3 CHARACTERIZATION
REMARK 1 REF J.BIOL.CHEM. V. 269 21177 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 30018
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3653
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.380
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.180
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 FOR RESIDUE LEU 452 THE ELECTRON DENSITY IS LARGER THAN
REMARK 3 EXPECTED.
REMARK 4
REMARK 4 1GCB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173513.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL; NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : SSRL; NULL
REMARK 200 BEAMLINE : BL7-1; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08; 1.54
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MSC, CCP4
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31451
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.07400
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: NULL; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 44.94000
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 44.94000
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 44.94000
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 44.94000
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 44.94000
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 44.94000
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: SYMMETRY
REMARK 300 THE CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS PRESENTED
REMARK 300 BELOW GENERATE THE SUBUNITS OF THE POLYMERIC MOLECULE.
REMARK 300
REMARK 300 APPLIED TO RESIDUES: 2 .. 453
REMARK 300
REMARK 300 IDENTITY MATRIX
REMARK 300
REMARK 300 SYMMETRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 300 SYMMETRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 300 SYMMETRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 300 SYMMETRY1 2 1.000000 0.000000 0.000000 0.00000
REMARK 300 SYMMETRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 300 SYMMETRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 300 APPLIED TO RESIDUES: 2 .. 453
REMARK 300
REMARK 300 MONOMER 2 OF HEXAMER
REMARK 300
REMARK 300 SYMMETRY1 3 0.000000 -1.000000 0.000000 1.00000
REMARK 300 SYMMETRY2 3 1.000000 -1.000000 0.000000 0.00000
REMARK 300 SYMMETRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 300 SYMMETRY1 4 -0.500000 -0.866000 0.000000 151.15000
REMARK 300 SYMMETRY2 4 0.866000 -0.500000 0.000000 0.00000
REMARK 300 SYMMETRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 300 APPLIED TO RESIDUES: 2 .. 453
REMARK 300
REMARK 300 MONOMER 3 OF HEXAMER
REMARK 300
REMARK 300 SYMMETRY1 5 -1.000000 1.000000 0.000000 1.00000
REMARK 300 SYMMETRY2 5 -1.000000 0.000000 0.000000 1.00000
REMARK 300 SYMMETRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 300 SYMMETRY1 6 -0.500000 0.866000 0.000000 75.58000
REMARK 300 SYMMETRY2 6 -0.866000 -0.500000 0.000000 130.90000
REMARK 300 SYMMETRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 300 APPLIED TO RESIDUES: 2 .. 453
REMARK 300
REMARK 300 MONOMER 4 OF HEXAMER
REMARK 300
REMARK 300 SYMMETRY1 7 0.000000 -1.000000 0.000000 1.00000
REMARK 300 SYMMETRY2 7 -1.000000 0.000000 0.000000 1.00000
REMARK 300 SYMMETRY3 7 0.000000 0.000000 -1.000000 0.50000
REMARK 300 SYMMETRY1 8 0.500000 -0.866000 0.000000 75.58000
REMARK 300 SYMMETRY2 8 -0.866000 -0.500000 0.000000 130.90000
REMARK 300 SYMMETRY3 8 0.000000 0.000000 -1.000000 44.94000
REMARK 300 APPLIED TO RESIDUES: 2 .. 453
REMARK 300
REMARK 300 MONOMER 5 OF HEXAMER (DIMER PARTNER OF MONOMER 1)
REMARK 300
REMARK 300 SYMMETRY1 9 1.000000 0.000000 0.000000 0.00000
REMARK 300 SYMMETRY2 9 1.000000 -1.000000 0.000000 0.00000
REMARK 300 SYMMETRY3 9 0.000000 0.000000 -1.000000 0.50000
REMARK 300 SYMMETRY1 10 0.500000 0.866000 0.000000 0.00000
REMARK 300 SYMMETRY2 10 0.866000 -0.500000 0.000000 0.00000
REMARK 300 SYMMETRY3 10 0.000000 0.000000 -1.000000 44.94000
REMARK 300 APPLIED TO RESIDUES: 2 .. 453
REMARK 300
REMARK 300 MONOMER 6 OF HEXAMER
REMARK 300
REMARK 300 SYMMETRY1 11 -1.000000 1.000000 0.000000 1.00000
REMARK 300 SYMMETRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 300 SYMMETRY3 11 0.000000 0.000000 -1.000000 0.50000
REMARK 300 SYMMETRY1 12 -1.000000 0.000000 0.000000 151.15000
REMARK 300 SYMMETRY2 12 0.000000 1.000000 0.000000 0.00000
REMARK 300 SYMMETRY3 12 0.000000 0.000000 -1.000000 44.94000
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: 42180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 95990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -742.0 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 151.15000
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 75.57500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 130.89974
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 75.57500
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 130.89974
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 44.94000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 151.15000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 44.94000
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 44.94000
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 MET A 1
REMARK 465 LYS A 454
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLU A 380
REMARK 475 THR A 381
REMARK 475 SER A 382
REMARK 475 LYS A 383
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 GLU A 89 CD OE1 OE2
REMARK 480 LYS A 93 NZ
REMARK 480 ARG A 174 NE CZ NH1 NH2
REMARK 480 GLU A 197 CB CG CD OE1 OE2
REMARK 480 ARG A 198 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 281 CD CE NZ
REMARK 480 LYS A 309 CE NZ
REMARK 480 LYS A 313 CG CD CE NZ
REMARK 480 ASN A 423 CG OD1 ND2
REMARK 480 LYS A 427 CD CE NZ
REMARK 480 GLU A 428 CB CG CD OE1 OE2
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 SER A 61 91.03 -66.16
REMARK 500 LYS A 68 -144.72 58.55
REMARK 500 TYR A 163 101.53 -166.82
REMARK 500 ALA A 172 68.43 -153.48
REMARK 500 ARG A 287 -9.63 60.17
REMARK 500 ASN A 290 -49.28 -139.50
REMARK 500 GLU A 380 79.81 -66.95
REMARK 500 THR A 381 -83.20 -174.30
REMARK 500 SER A 382 18.40 -162.88
REMARK 500 LYS A 383 -138.90 -97.79
REMARK 500 SER A 435 -139.27 -83.47
REMARK 500 GLU A 438 91.02 -58.87
REMARK 500 LEU A 452 -159.39 -49.04
REMARK 500
REMARK 500 REMARK: NULL
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 HG A 902 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 55 OG1
REMARK 620 2 CYS A 376 SG 50.0
REMARK 620 3 VAL A 378 N 108.6 125.7
REMARK 620 4 HG A 903 HG 113.6 64.8 118.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 904 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 73 SG
REMARK 620 2 ALA A 453 O 69.2
REMARK 620 N 1
REMARK 700
REMARK 700 SHEET
REMARK 700 IN THE SHEET RECORDS BELOW STRAND 7 OF SHEET B IS REPEATED
REMARK 700 IN SHEET C BECAUSE IT TAKES PART IN BOTH SHEETS.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 851
DBREF 1GCB A 1 454 UNP Q01532 BLH1_YEAST 1 454
SEQRES 1 A 454 MET SER SER SER ILE ASP ILE SER LYS ILE ASN SER TRP
SEQRES 2 A 454 ASN LYS GLU PHE GLN SER ASP LEU THR HIS GLN LEU ALA
SEQRES 3 A 454 THR THR VAL LEU LYS ASN TYR ASN ALA ASP ASP ALA LEU
SEQRES 4 A 454 LEU ASN LYS THR ARG LEU GLN LYS GLN ASP ASN ARG VAL
SEQRES 5 A 454 PHE ASN THR VAL VAL SER THR ASP SER THR PRO VAL THR
SEQRES 6 A 454 ASN GLN LYS SER SER GLY ARG CYS TRP LEU PHE ALA ALA
SEQRES 7 A 454 THR ASN GLN LEU ARG LEU ASN VAL LEU SER GLU LEU ASN
SEQRES 8 A 454 LEU LYS GLU PHE GLU LEU SER GLN ALA TYR LEU PHE PHE
SEQRES 9 A 454 TYR ASP LYS LEU GLU LYS ALA ASN TYR PHE LEU ASP GLN
SEQRES 10 A 454 ILE VAL SER SER ALA ASP GLN ASP ILE ASP SER ARG LEU
SEQRES 11 A 454 VAL GLN TYR LEU LEU ALA ALA PRO THR GLU ASP GLY GLY
SEQRES 12 A 454 GLN TYR SER MET PHE LEU ASN LEU VAL LYS LYS TYR GLY
SEQRES 13 A 454 LEU ILE PRO LYS ASP LEU TYR GLY ASP LEU PRO TYR SER
SEQRES 14 A 454 THR THR ALA SER ARG LYS TRP ASN SER LEU LEU THR THR
SEQRES 15 A 454 LYS LEU ARG GLU PHE ALA GLU THR LEU ARG THR ALA LEU
SEQRES 16 A 454 LYS GLU ARG SER ALA ASP ASP SER ILE ILE VAL THR LEU
SEQRES 17 A 454 ARG GLU GLN MET GLN ARG GLU ILE PHE ARG LEU MET SER
SEQRES 18 A 454 LEU PHE MET ASP ILE PRO PRO VAL GLN PRO ASN GLU GLN
SEQRES 19 A 454 PHE THR TRP GLU TYR VAL ASP LYS ASP LYS LYS ILE HIS
SEQRES 20 A 454 THR ILE LYS SER THR PRO LEU GLU PHE ALA SER LYS TYR
SEQRES 21 A 454 ALA LYS LEU ASP PRO SER THR PRO VAL SER LEU ILE ASN
SEQRES 22 A 454 ASP PRO ARG HIS PRO TYR GLY LYS LEU ILE LYS ILE ASP
SEQRES 23 A 454 ARG LEU GLY ASN VAL LEU GLY GLY ASP ALA VAL ILE TYR
SEQRES 24 A 454 LEU ASN VAL ASP ASN GLU THR LEU SER LYS LEU VAL VAL
SEQRES 25 A 454 LYS ARG LEU GLN ASN ASN LYS ALA VAL PHE PHE GLY SER
SEQRES 26 A 454 HIS THR PRO LYS PHE MET ASP LYS LYS THR GLY VAL MET
SEQRES 27 A 454 ASP ILE GLU LEU TRP ASN TYR PRO ALA ILE GLY TYR ASN
SEQRES 28 A 454 LEU PRO GLN GLN LYS ALA SER ARG ILE ARG TYR HIS GLU
SEQRES 29 A 454 SER LEU MET THR HIS ALA MET LEU ILE THR GLY CYS HIS
SEQRES 30 A 454 VAL ASP GLU THR SER LYS LEU PRO LEU ARG TYR ARG VAL
SEQRES 31 A 454 GLU ASN SER TRP GLY LYS ASP SER GLY LYS ASP GLY LEU
SEQRES 32 A 454 TYR VAL MET THR GLN LYS TYR PHE GLU GLU TYR CYS PHE
SEQRES 33 A 454 GLN ILE VAL VAL ASP ILE ASN GLU LEU PRO LYS GLU LEU
SEQRES 34 A 454 ALA SER LYS PHE THR SER GLY LYS GLU GLU PRO ILE VAL
SEQRES 35 A 454 LEU PRO ILE TRP ASP PRO MET GLY ALA LEU ALA LYS
HET SO4 A 801 5
HET SO4 A 802 5
HET SO4 A 803 5
HET HG A 901 1
HET HG A 902 1
HET HG A 903 1
HET HG A 904 1
HET GOL A 851 6
HETNAM SO4 SULFATE ION
HETNAM HG MERCURY (II) ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 HG 4(HG 2+)
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *238(H2 O)
HELIX 1 1 ILE A 7 SER A 19 1 13
HELIX 2 2 LEU A 21 LEU A 30 1 10
HELIX 3 3 ALA A 35 LEU A 39 1 5
HELIX 4 4 LYS A 42 GLN A 48 1 7
HELIX 5 5 CYS A 73 GLU A 89 1 17
HELIX 6 6 GLN A 99 SER A 121 1 23
HELIX 7 7 ARG A 129 ALA A 136 1 8
HELIX 8 8 TYR A 145 TYR A 155 1 11
HELIX 9 9 LYS A 160 LEU A 162 5 3
HELIX 10 10 TYR A 168 THR A 171 1 4
HELIX 11 11 ARG A 174 GLU A 197 1 24
HELIX 12 12 SER A 203 PHE A 223 1 21
HELIX 13 13 PRO A 253 LYS A 259 1 7
HELIX 14 14 ASN A 304 GLN A 316 1 13
HELIX 15 15 TYR A 345 ILE A 348 5 4
HELIX 16 16 LYS A 356 ARG A 361 1 6
HELIX 17 17 GLN A 408 TYR A 414 1 7
HELIX 18 18 ILE A 422 GLU A 424 5 3
HELIX 19 19 LYS A 427 THR A 434 1 8
SHEET 1 A 2 GLN A 234 VAL A 240 0
SHEET 2 A 2 ILE A 246 THR A 252 -1 N SER A 251 O PHE A 235
SHEET 1 B11 ILE A 441 LEU A 443 0
SHEET 2 B11 LEU A 282 ILE A 285 1 N LYS A 284 O ILE A 441
SHEET 3 B11 ILE A 298 ASN A 301 -1 N TYR A 299 O ILE A 283
SHEET 4 B11 PRO A 268 ILE A 272 1 N SER A 270 O LEU A 300
SHEET 5 B11 CYS A 415 ASP A 421 -1 N VAL A 420 O VAL A 269
SHEET 6 B11 VAL A 321 SER A 325 -1 N GLY A 324 O PHE A 416
SHEET 7 B11 HIS A 369 HIS A 377 -1 N ILE A 373 O VAL A 321
SHEET 8 B11 ARG A 387 GLU A 391 -1 N GLU A 391 O LEU A 372
SHEET 9 B11 LEU A 403 THR A 407 -1 N MET A 406 O TYR A 388
SHEET 10 B11 GLY A 336 ASP A 339 1 N MET A 338 O VAL A 405
SHEET 11 B11 PHE A 330 LYS A 333 -1 N ASP A 332 O VAL A 337
SHEET 1 C 2 THR A 55 VAL A 57 0
SHEET 2 C 2 HIS A 369 HIS A 377 -1 N CYS A 376 O THR A 55
LINK OG1 THR A 55 HG HG A 902 1555 1555 3.24
LINK SG CYS A 73 HG HG A 904 1555 1555 2.12
LINK SG CYS A 376 HG HG A 902 1555 1555 2.19
LINK SG CYS A 376 HG HG A 903 1555 1555 2.61
LINK N VAL A 378 HG HG A 902 1555 1555 3.15
LINK SG CYS A 415 HG HG A 901 1555 1555 2.53
LINK O ALA A 453 HG HG A 904 1555 1555 3.52
LINK HG HG A 902 HG HG A 903 1555 1555 2.64
CISPEP 1 THR A 62 PRO A 63 0 -0.03
CISPEP 2 THR A 327 PRO A 328 0 -0.52
SITE 1 CAT 3 CYS A 73 HIS A 369 ASN A 392
SITE 1 AC1 5 ASN A 66 GLY A 395 LYS A 396 HOH A 675
SITE 2 AC1 5 HOH A 714
SITE 1 AC2 6 ILE A 126 ARG A 192 LYS A 196 TYR A 362
SITE 2 AC2 6 HOH A 643 HOH A 644
SITE 1 AC3 7 LYS A 175 SER A 178 PRO A 328 LYS A 329
SITE 2 AC3 7 HOH A 691 HOH A 697 HOH A 698
SITE 1 AC4 2 PHE A 411 CYS A 415
SITE 1 AC5 4 THR A 55 CYS A 376 VAL A 378 HG A 903
SITE 1 AC6 4 VAL A 312 CYS A 376 PRO A 385 HG A 902
SITE 1 AC7 3 GLY A 71 CYS A 73 ALA A 453
SITE 1 AC8 8 GLN A 81 LEU A 82 ASN A 85 LYS A 262
SITE 2 AC8 8 ARG A 314 LYS A 319 ASP A 421 HOH A 684
CRYST1 151.150 151.150 89.880 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 0.006616 0.003820 0.000000 0.00000
SCALE2 0.000000 0.007639 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011126 0.00000
(ATOM LINES ARE NOT SHOWN.)
END