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HEADER HYDROLASE 01-JUL-04 1WM1
TITLE CRYSTAL STRUCTURE OF PROLYL AMINOPEPTIDASE, COMPLEX WITH
TITLE 2 PRO-TBODA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE IMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIP, PROLYL AMINOPEPTIDASE, PAP;
COMPND 5 EC: 3.4.11.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SERRATIA MARCESCENS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS PROLINE IMINOPEPTIDASE, COMPLEX WITH INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NAKAJIMA,T.INOUE,K.ITO,T.TOZAKA,S.HATAKEYAMA,N.TANAKA,
AUTHOR 2 K.T.NAKAMURA,T.YOSHIMOTO
REVDAT 1 20-JUL-04 1WM1 0
JRNL AUTH T.INOUE,K.ITO,T.TOZAKA,S.HATAKEYAMA,N.TANAKA,
JRNL AUTH 2 K.T.NAKAMURA,T.YOSHIMOTO
JRNL TITL NOVEL INHIBITOR FOR PROLYL AMINOPEPTIDASE FROM
JRNL TITL 2 SERRATIA MARCESCENS AND STUDIES ON THE MECHANISM
JRNL TITL 3 OF SUBSTRATE RECOGNITION OF THE ENZYME USING THE
JRNL TITL 4 INHIBITOR
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 416 147 2003
JRNL REFN ASTM ABBIA4 US ISSN 0003-9861
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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 : 22269
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) : 0.200
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1139
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.2881
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 98
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 : 2520
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 73
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.32
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.72
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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WM1 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-2004.
REMARK 100 THE RCSB ID CODE IS RCSB023727.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-2003
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22338
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22800
REMARK 200 FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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 (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, CACODYLATE, SODIUM
REMARK 280 ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,1/2-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.53550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 32.72250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 32.72250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 126.80325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 32.72250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 32.72250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.26775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 32.72250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.72250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 126.80325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 32.72250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 32.72250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.26775
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 84.53550
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 GLU A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 317
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 ARG A 145 CG ARG A 145 CD -0.034
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 ARG A 26 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 LYS A 65 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 GLY A 73 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 PRO A 79 C - N - CA ANGL. DEV. = 7.2 DEGREES
REMARK 500 VAL A 134 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 LEU A 141 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 TYR A 150 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP A 222 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP A 268 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 ILE A 290 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 SER A 297 N - CA - C ANGL. DEV. = 7.0 DEGREES
REMARK 500 GLU A 300 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QTR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
DBREF 1WM1 A 1 317 SWS O32449 PIP_SERMA 1 317
SEQRES 1 A 317 MET GLU GLN LEU ARG GLY LEU TYR PRO PRO LEU ALA ALA
SEQRES 2 A 317 TYR ASP SER GLY TRP LEU ASP THR GLY ASP GLY HIS ARG
SEQRES 3 A 317 ILE TYR TRP GLU LEU SER GLY ASN PRO ASN GLY LYS PRO
SEQRES 4 A 317 ALA VAL PHE ILE HIS GLY GLY PRO GLY GLY GLY ILE SER
SEQRES 5 A 317 PRO HIS HIS ARG GLN LEU PHE ASP PRO GLU ARG TYR LYS
SEQRES 6 A 317 VAL LEU LEU PHE ASP GLN ARG GLY CYS GLY ARG SER ARG
SEQRES 7 A 317 PRO HIS ALA SER LEU ASP ASN ASN THR THR TRP HIS LEU
SEQRES 8 A 317 VAL ALA ASP ILE GLU ARG LEU ARG GLU MET ALA GLY VAL
SEQRES 9 A 317 GLU GLN TRP LEU VAL PHE GLY GLY SER TRP GLY SER THR
SEQRES 10 A 317 LEU ALA LEU ALA TYR ALA GLN THR HIS PRO GLU ARG VAL
SEQRES 11 A 317 SER GLU MET VAL LEU ARG GLY ILE PHE THR LEU ARG LYS
SEQRES 12 A 317 GLN ARG LEU HIS TRP TYR TYR GLN ASP GLY ALA SER ARG
SEQRES 13 A 317 PHE PHE PRO GLU LYS TRP GLU ARG VAL LEU SER ILE LEU
SEQRES 14 A 317 SER ASP ASP GLU ARG LYS ASP VAL ILE ALA ALA TYR ARG
SEQRES 15 A 317 GLN ARG LEU THR SER ALA ASP PRO GLN VAL GLN LEU GLU
SEQRES 16 A 317 ALA ALA LYS LEU TRP SER VAL TRP GLU GLY GLU THR VAL
SEQRES 17 A 317 THR LEU LEU PRO SER ARG GLU SER ALA SER PHE GLY GLU
SEQRES 18 A 317 ASP ASP PHE ALA LEU ALA PHE ALA ARG ILE GLU ASN HIS
SEQRES 19 A 317 TYR PHE THR HIS LEU GLY PHE LEU GLU SER ASP ASP GLN
SEQRES 20 A 317 LEU LEU ARG ASN VAL PRO LEU ILE ARG HIS ILE PRO ALA
SEQRES 21 A 317 VAL ILE VAL HIS GLY ARG TYR ASP MET ALA CYS GLN VAL
SEQRES 22 A 317 GLN ASN ALA TRP ASP LEU ALA LYS ALA TRP PRO GLU ALA
SEQRES 23 A 317 GLU LEU HIS ILE VAL GLU GLY ALA GLY HIS SER TYR ASP
SEQRES 24 A 317 GLU PRO GLY ILE LEU HIS GLN LEU MET ILE ALA THR ASP
SEQRES 25 A 317 ARG PHE ALA GLY LYS
HET PTB 401 16
HETNAM PTB (5-TERT-BUTYL-1,3,4-OXADIAZOL-2-YL)[(2R)-PYRROLIDIN-2-
HETNAM 2 PTB YL]METHANONE
HETSYN PTB 2-PROLYL-5-TERT-BUTYL-[1,3,4]OXADIAZOLE
FORMUL 2 PTB C11 H17 N3 O2
FORMUL 3 HOH *73(H2 O1)
HELIX 1 1 SER A 52 PHE A 59 5 8
HELIX 2 2 THR A 87 ALA A 102 1 16
HELIX 3 3 SER A 113 HIS A 126 1 14
HELIX 4 4 ARG A 142 GLN A 151 1 10
HELIX 5 5 GLY A 153 PHE A 157 5 5
HELIX 6 6 PHE A 158 SER A 167 1 10
HELIX 7 7 ASP A 172 LYS A 175 5 4
HELIX 8 8 ASP A 176 THR A 186 1 11
HELIX 9 9 ASP A 189 GLU A 206 1 18
HELIX 10 10 ARG A 214 GLY A 220 5 7
HELIX 11 11 GLU A 221 HIS A 238 1 18
HELIX 12 12 LEU A 239 LEU A 242 5 4
HELIX 13 13 ASP A 246 ASN A 251 1 6
HELIX 14 14 VAL A 252 ILE A 255 5 4
HELIX 15 15 GLN A 272 TRP A 283 1 12
HELIX 16 16 GLU A 300 ALA A 315 1 16
SHEET 1 A 8 ASP A 15 ASP A 20 0
SHEET 2 A 8 ARG A 26 GLY A 33 -1 O LEU A 31 N ASP A 15
SHEET 3 A 8 TYR A 64 PHE A 69 -1 O VAL A 66 N SER A 32
SHEET 4 A 8 LYS A 38 ILE A 43 1 N LYS A 38 O LYS A 65
SHEET 5 A 8 TRP A 107 GLY A 112 1 O PHE A 110 N ILE A 43
SHEET 6 A 8 VAL A 130 ARG A 136 1 O GLU A 132 N VAL A 109
SHEET 7 A 8 ALA A 260 GLY A 265 1 O VAL A 261 N LEU A 135
SHEET 8 A 8 GLU A 287 VAL A 291 1 O GLU A 287 N ILE A 262
CISPEP 1 GLY A 46 PRO A 47 0 -0.08
CISPEP 2 ARG A 78 PRO A 79 0 0.18
CRYST1 65.445 65.445 169.071 90.00 90.00 90.00 P 43 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 0.015280 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005915 0.00000
TER 2521 GLY A 316
MASTER 282 0 1 16 8 0 0 6 2609 1 16 25
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