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HEADER HYDROLASE 15-OCT-04 1XRQ
TITLE CRYSTAL STRUCTURE OF ACTIVE SITE F1-MUTANT E245Q SOAKED
TITLE 2 WITH PEPTIDE PHE-LEU
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE IMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIP, PROLYL AMINOPEPTIDASE, PAP, TRICORN PROTEASE
COMPND 5 INTERACTING FACTOR F1;
COMPND 6 EC: 3.4.11.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 GENE: TA0830;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET6C
KEYWDS ALPHA-BETA HYDROLASE, CAGED ACTIVE SITE, SUBSTRATE
KEYWDS 2 RECOGNITION, HYDROGEN BONDED NETWORK, PEPTIDE CLEAVAGE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GOETTIG,H.BRANDSTETTER,M.GROLL,W.GOEHRING,P.V.KONAREV,
AUTHOR 2 D.I.SVERGUN,R.HUBER,J.-S.KIM
REVDAT 2 24-JAN-06 1XRQ 1 JRNL
REVDAT 1 12-JUL-05 1XRQ 0
JRNL AUTH P.GOETTIG,H.BRANDSTETTER,M.GROLL,W.GOEHRING,
JRNL AUTH 2 P.V.KONAREV,D.I.SVERGUN,R.HUBER,J.-S.KIM
JRNL TITL X-RAY SNAPSHOTS OF PEPTIDE PROCESSING IN MUTANTS
JRNL TITL 2 OF TRICORN-INTERACTING FACTOR F1 FROM THERMOPLASMA
JRNL TITL 3 ACIDOPHILUM
JRNL REF J.BIOL.CHEM. V. 280 33387 2005
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1056834.870
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 6889
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) : 0.204
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.600
REMARK 3 FREE R VALUE TEST SET COUNT : 384
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.015
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 59.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 680
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE : 0.4310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 40
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.068
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2328
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 30
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.91000
REMARK 3 B22 (A**2) : 9.48000
REMARK 3 B33 (A**2) : -10.39000
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) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.46
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) : 0.47
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.63
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) : 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 : 33.64
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 1XRQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-OCT-2004.
REMARK 100 THE RCSB ID CODE IS RCSB030689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
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 : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6902
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.780
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 59.4
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, BIS-TRIS, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 28.78000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.01500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.95500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.01500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.78000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.95500
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 MET A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
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 GLU A 4 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 51 SD MET A 51 CE 0.058
REMARK 500 MET A 208 SD MET A 208 CE 0.069
REMARK 500 GLN A 245 CD GLN A 245 NE2 -0.074
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 9 N - CA - C ANGL. DEV. = -6.8 DEGREES
REMARK 500 VAL A 246 N - CA - C ANGL. DEV. = -8.6 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 185 62.55 0.62
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 25 DISTANCE = 5.01 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MTZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRICORN INTERACTING FACTOR F1
REMARK 900 RELATED ID: 1MU0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRICORN INTERACTING FACTOR F1
REMARK 900 COMPLEX WITH PCK
REMARK 900 RELATED ID: 1MT3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRICORN INTERACTING FACTOR
REMARK 900 SELENOMETHIONINE-F1
REMARK 900 RELATED ID: 1XQV RELATED DB: PDB
REMARK 900 THE SAME PROTEIN G37A MUTANT
REMARK 900 RELATED ID: 1XQW RELATED DB: PDB
REMARK 900 THE SAME PROTEIN S105A MUTANT COMPLEX WITH PHE-LEU
REMARK 900 RELATED ID: 1XQX RELATED DB: PDB
REMARK 900 THE SAME PROTEIN S105A MUTANT COMPLEX WITH PCK
REMARK 900 RELATED ID: 1XQY RELATED DB: PDB
REMARK 900 THE SAME PROTEIN S105A MUTANT COMPLEX WITH PRO-LEU-GLY-GLY
REMARK 900 RELATED ID: 1XRL RELATED DB: PDB
REMARK 900 THE SAME PROTEIN Y205F MUTANT COMPLEX WITH INHIBITOR PCK
REMARK 900 RELATED ID: 1XRM RELATED DB: PDB
REMARK 900 THE SAME PROTEIN E213Q MUTANT SOAKED WITH PEPTIDE ALA-PHE
REMARK 900 RELATED ID: 1XRN RELATED DB: PDB
REMARK 900 THE SAME PROTEIN E213Q MUTANT SOAKED WITH PEPTIDE PHE-ALA
REMARK 900 RELATED ID: 1XRO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN E213Q MUTANT SOAKED WITH PEPTIDE PHE-LEU
REMARK 900 RELATED ID: 1XRP RELATED DB: PDB
REMARK 900 THE SAME PROTEIN E213Q MUTANT SOAKED WITH PEPTIDE PRO-LEU-
REMARK 900 GLY-GLY
REMARK 900 RELATED ID: 1XRR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN E245Q MUTANT SOAKED WITH PEPTIDE PRO-PRO
DBREF 1XRQ A 1 293 SWS P96084 PIP_THEAC 1 293
SEQADV 1XRQ GLN A 245 SWS P96084 GLU 245 ENGINEERED
SEQRES 1 A 293 MET ASP GLN GLU CYS ILE GLU ASN TYR ALA LYS VAL ASN
SEQRES 2 A 293 GLY ILE TYR ILE TYR TYR LYS LEU CYS LYS ALA PRO GLU
SEQRES 3 A 293 GLU LYS ALA LYS LEU MET THR MET HIS GLY GLY PRO GLY
SEQRES 4 A 293 MET SER HIS ASP TYR LEU LEU SER LEU ARG ASP MET THR
SEQRES 5 A 293 LYS GLU GLY ILE THR VAL LEU PHE TYR ASP GLN PHE GLY
SEQRES 6 A 293 CYS GLY ARG SER GLU GLU PRO ASP GLN SER LYS PHE THR
SEQRES 7 A 293 ILE ASP TYR GLY VAL GLU GLU ALA GLU ALA LEU ARG SER
SEQRES 8 A 293 LYS LEU PHE GLY ASN GLU LYS VAL PHE LEU MET GLY SER
SEQRES 9 A 293 SER TYR GLY GLY ALA LEU ALA LEU ALA TYR ALA VAL LYS
SEQRES 10 A 293 TYR GLN ASP HIS LEU LYS GLY LEU ILE VAL SER GLY GLY
SEQRES 11 A 293 LEU SER SER VAL PRO LEU THR VAL LYS GLU MET ASN ARG
SEQRES 12 A 293 LEU ILE ASP GLU LEU PRO ALA LYS TYR ARG ASP ALA ILE
SEQRES 13 A 293 LYS LYS TYR GLY SER SER GLY SER TYR GLU ASN PRO GLU
SEQRES 14 A 293 TYR GLN GLU ALA VAL ASN TYR PHE TYR HIS GLN HIS LEU
SEQRES 15 A 293 LEU ARG SER GLU ASP TRP PRO PRO GLU VAL LEU LYS SER
SEQRES 16 A 293 LEU GLU TYR ALA GLU ARG ARG ASN VAL TYR ARG ILE MET
SEQRES 17 A 293 ASN GLY PRO ASN GLU PHE THR ILE THR GLY THR ILE LYS
SEQRES 18 A 293 ASP TRP ASP ILE THR ASP LYS ILE SER ALA ILE LYS ILE
SEQRES 19 A 293 PRO THR LEU ILE THR VAL GLY GLU TYR ASP GLN VAL THR
SEQRES 20 A 293 PRO ASN VAL ALA ARG VAL ILE HIS GLU LYS ILE ALA GLY
SEQRES 21 A 293 SER GLU LEU HIS VAL PHE ARG ASP CYS SER HIS LEU THR
SEQRES 22 A 293 MET TRP GLU ASP ARG GLU GLY TYR ASN LYS LEU LEU SER
SEQRES 23 A 293 ASP PHE ILE LEU LYS HIS LEU
HET LEU 301 9
HETNAM LEU LEUCINE
FORMUL 2 LEU C6 H13 N1 O2
FORMUL 3 HOH *30(H2 O1)
HELIX 1 1 SER A 41 GLU A 54 5 14
HELIX 2 2 ASP A 73 PHE A 77 5 5
HELIX 3 3 THR A 78 GLY A 95 1 18
HELIX 4 4 SER A 105 GLN A 119 1 15
HELIX 5 5 SER A 133 LEU A 148 1 16
HELIX 6 6 PRO A 149 SER A 162 1 14
HELIX 7 7 ASN A 167 LEU A 182 1 16
HELIX 8 8 PRO A 189 GLU A 200 1 12
HELIX 9 9 ASN A 203 ASN A 209 1 7
HELIX 10 10 GLY A 218 TRP A 223 5 6
HELIX 11 11 ILE A 225 SER A 230 1 6
HELIX 12 12 THR A 247 ILE A 258 1 12
HELIX 13 13 LEU A 272 ASP A 277 1 6
HELIX 14 14 ASP A 277 HIS A 292 1 16
SHEET 1 A 8 ILE A 6 VAL A 12 0
SHEET 2 A 8 ILE A 15 CYS A 22 -1 O ILE A 17 N ALA A 10
SHEET 3 A 8 ILE A 56 TYR A 61 -1 O PHE A 60 N LYS A 20
SHEET 4 A 8 ALA A 29 MET A 34 1 N LEU A 31 O THR A 57
SHEET 5 A 8 VAL A 99 SER A 104 1 O PHE A 100 N MET A 32
SHEET 6 A 8 LEU A 122 SER A 128 1 O ILE A 126 N LEU A 101
SHEET 7 A 8 THR A 236 GLY A 241 1 O LEU A 237 N LEU A 125
SHEET 8 A 8 GLU A 262 PHE A 266 1 O PHE A 266 N VAL A 240
SSBOND 1 CYS A 5 CYS A 22
CISPEP 1 GLY A 37 PRO A 38 0 -0.21
CRYST1 57.560 61.910 80.030 90.00 90.00 90.00 P 21 21 21 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 0.017373 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016152 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012495 0.00000
TER 2329 LEU A 293
MASTER 317 0 1 14 8 0 0 6 2367 1 2 23
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