HEADER TRANSFERASE 30-AUG-02 1ML4
TITLE THE PALA-LIGANDED ASPARTATE TRANSCARBAMOYLASE CATALYTIC SUBUNIT FROM
TITLE 2 PYROCOCCUS ABYSSI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE TRANSCARBAMOYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ASPARTATE CARBAMOYLTRANSFERASE;
COMPND 5 EC: 2.1.3.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS ABYSSI;
SOURCE 3 ORGANISM_TAXID: 29292;
SOURCE 4 GENE: PYRB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C600ATC-;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS BETA PLEATED SHEET, PROTEIN INHIBITOR COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.VAN BOXSTAEL,R.CUNIN,D.MAES
REVDAT 4 25-OCT-23 1ML4 1 REMARK
REVDAT 3 13-JUL-11 1ML4 1 VERSN
REVDAT 2 24-FEB-09 1ML4 1 VERSN
REVDAT 1 25-FEB-03 1ML4 0
JRNL AUTH S.VAN BOXSTAEL,R.CUNIN,S.KHAN,D.MAES
JRNL TITL ASPARTATE TRANSCARBAMYLASE FROM THE HYPERTHERMOPHILIC
JRNL TITL 2 ARCHAEON PYROCOCCUS ABYSSI: THERMOSTABILITY AND 1.8A
JRNL TITL 3 RESOLUTION CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT
JRNL TITL 4 COMPLEXED WITH THE BISUBSTRATE ANALOGUE
JRNL TITL 5 N-PHOSPHONACETYL-L-ASPARTATE.
JRNL REF J.MOL.BIOL. V. 326 203 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12547202
JRNL DOI 10.1016/S0022-2836(02)01228-7
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
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) (%) : 88.6
REMARK 3 NUMBER OF REFLECTIONS : 28560
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : RFREE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2651
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2924
REMARK 3 BIN FREE R VALUE : 0.2816
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 251
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 : 2450
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 77
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.63900
REMARK 3 B22 (A**2) : -4.63900
REMARK 3 B33 (A**2) : 9.27900
REMARK 3 B12 (A**2) : -3.45000
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) : 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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.290
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.096 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.784 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.741 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.556 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CNS VERSION FOR HEMIHEDRAL TWINNED DATA
REMARK 4
REMARK 4 1ML4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000016996.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.84
REMARK 200 MONOCHROMATOR : TRIANGULAR MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29667
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : 2.380
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.33000
REMARK 200 R SYM FOR SHELL (I) : 0.33000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.910
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB 1EKX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRIC ACID, PH 6.8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 40.54750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.41011
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 47.31967
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 40.54750
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 23.41011
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 47.31967
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 40.54750
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 23.41011
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 47.31967
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.82022
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 94.63933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 46.82022
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 94.63933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 46.82022
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 94.63933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 TRIMER GENERATED BY THE
REMARK 300 OPERATIONS : -Y,X-Y,Z AND -X+Y,-X,Z
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: TRIMERIC
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 0.00000
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 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
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 40.54750
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 70.23033
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -40.54750
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 70.23033
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 401 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 404 LIES ON A SPECIAL POSITION.
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 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 ASP A 2 N
REMARK 480 ARG A 12 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 34 NZ
REMARK 480 LYS A 43 CE NZ
REMARK 480 ARG A 193 CG
REMARK 480 ARG A 196 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 204 CB CG OE1 OE2
REMARK 480 LYS A 221 CG CD CE NZ
REMARK 480 ARG A 288 CG CD NE 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 GLN A 38 112.82 -178.89
REMARK 500 ASN A 133 -85.78 -76.63
REMARK 500 HIS A 135 69.62 -154.32
REMARK 500 ILE A 153 -77.57 -67.43
REMARK 500 GLN A 231 61.33 -67.51
REMARK 500 TYR A 248 145.69 176.32
REMARK 500 LYS A 257 31.23 -95.69
REMARK 500 LEU A 268 160.14 69.38
REMARK 500 VAL A 271 -71.69 -98.19
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 PAL A 385
DBREF 1ML4 A 1 308 UNP P77918 PYRB_PYRAB 1 308
SEQRES 1 A 308 MET ASP TRP LYS GLY ARG ASP VAL ILE SER ILE ARG ASP
SEQRES 2 A 308 PHE SER LYS GLU ASP ILE GLU THR VAL LEU ALA THR ALA
SEQRES 3 A 308 GLU ARG LEU GLU ARG GLU LEU LYS GLU LYS GLY GLN LEU
SEQRES 4 A 308 GLU TYR ALA LYS GLY LYS ILE LEU ALA THR LEU PHE PHE
SEQRES 5 A 308 GLU PRO SER THR ARG THR ARG LEU SER PHE GLU SER ALA
SEQRES 6 A 308 MET HIS ARG LEU GLY GLY ALA VAL ILE GLY PHE ALA GLU
SEQRES 7 A 308 ALA SER THR SER SER VAL LYS LYS GLY GLU SER LEU ARG
SEQRES 8 A 308 ASP THR ILE LYS THR VAL GLU GLN TYR CYS ASP VAL ILE
SEQRES 9 A 308 VAL ILE ARG HIS PRO LYS GLU GLY ALA ALA ARG LEU ALA
SEQRES 10 A 308 ALA GLU VAL ALA GLU VAL PRO VAL ILE ASN ALA GLY ASP
SEQRES 11 A 308 GLY SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU
SEQRES 12 A 308 TYR THR ILE LYS LYS GLU PHE GLY ARG ILE ASP GLY LEU
SEQRES 13 A 308 LYS ILE GLY LEU LEU GLY ASP LEU LYS TYR GLY ARG THR
SEQRES 14 A 308 VAL HIS SER LEU ALA GLU ALA LEU THR PHE TYR ASP VAL
SEQRES 15 A 308 GLU LEU TYR LEU ILE SER PRO GLU LEU LEU ARG MET PRO
SEQRES 16 A 308 ARG HIS ILE VAL GLU GLU LEU ARG GLU LYS GLY MET LYS
SEQRES 17 A 308 VAL VAL GLU THR THR THR LEU GLU ASP VAL ILE GLY LYS
SEQRES 18 A 308 LEU ASP VAL LEU TYR VAL THR ARG ILE GLN LYS GLU ARG
SEQRES 19 A 308 PHE PRO ASP GLU GLN GLU TYR LEU LYS VAL LYS GLY SER
SEQRES 20 A 308 TYR GLN VAL ASN LEU LYS VAL LEU GLU LYS ALA LYS ASP
SEQRES 21 A 308 GLU LEU ARG ILE MET HIS PRO LEU PRO ARG VAL ASP GLU
SEQRES 22 A 308 ILE HIS PRO GLU VAL ASP ASN THR LYS HIS ALA ILE TYR
SEQRES 23 A 308 PHE ARG GLN VAL PHE ASN GLY VAL PRO VAL ARG MET ALA
SEQRES 24 A 308 LEU LEU ALA LEU VAL LEU GLY VAL ILE
HET PAL A 385 16
HETNAM PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID
FORMUL 2 PAL C6 H10 N O8 P
FORMUL 3 HOH *77(H2 O)
HELIX 1 1 SER A 10 PHE A 14 5 5
HELIX 2 2 SER A 15 GLY A 37 1 23
HELIX 3 3 THR A 56 LEU A 69 1 14
HELIX 4 4 GLU A 78 GLY A 87 5 10
HELIX 5 5 SER A 89 GLU A 98 1 10
HELIX 6 6 GLY A 112 VAL A 120 1 9
HELIX 7 7 HIS A 135 PHE A 150 1 16
HELIX 8 8 GLY A 167 LEU A 177 1 11
HELIX 9 9 THR A 178 TYR A 180 5 3
HELIX 10 10 PRO A 189 ARG A 193 5 5
HELIX 11 11 PRO A 195 LYS A 205 1 11
HELIX 12 12 LEU A 215 GLY A 220 1 6
HELIX 13 13 GLN A 231 PHE A 235 5 5
HELIX 14 14 ASP A 237 LYS A 243 1 7
HELIX 15 15 LYS A 253 ALA A 258 5 6
HELIX 16 16 HIS A 275 THR A 281 5 7
HELIX 17 17 ILE A 285 ASN A 292 1 8
HELIX 18 18 ASN A 292 LEU A 305 1 14
SHEET 1 A 4 ALA A 72 PHE A 76 0
SHEET 2 A 4 ILE A 46 PHE A 51 1 N LEU A 47 O ALA A 72
SHEET 3 A 4 VAL A 103 HIS A 108 1 O VAL A 105 N LEU A 50
SHEET 4 A 4 VAL A 125 ASP A 130 1 O ILE A 126 N ILE A 104
SHEET 1 B 5 VAL A 209 THR A 212 0
SHEET 2 B 5 VAL A 182 ILE A 187 1 N LEU A 186 O VAL A 210
SHEET 3 B 5 LEU A 156 LEU A 161 1 N LEU A 160 O TYR A 185
SHEET 4 B 5 VAL A 224 VAL A 227 1 O VAL A 224 N GLY A 159
SHEET 5 B 5 ARG A 263 MET A 265 1 O MET A 265 N LEU A 225
CISPEP 1 LEU A 268 PRO A 269 0 -0.69
SITE 1 AC1 15 SER A 55 THR A 56 ARG A 57 THR A 58
SITE 2 AC1 15 SER A 83 LYS A 86 ARG A 107 HIS A 135
SITE 3 AC1 15 GLN A 138 ARG A 168 ARG A 229 GLN A 231
SITE 4 AC1 15 LEU A 268 HOH A 394 HOH A 395
CRYST1 81.095 81.095 141.959 90.00 90.00 120.00 H 3 9
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 0.012331 0.007119 0.000000 0.00000
SCALE2 0.000000 0.014239 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007044 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
