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HEADER HYDROLASE 03-MAY-02 1LNS
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE X-PROLYL DIPEPTIDYL
TITLE 2 AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: X-PROLYL DIPEPTIDYL AMINOPETIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: X-PRO DIPEPTIDYL-PEPTIDASE, XAA-PRO DIPEPTIDYL-
COMPND 5 PEPTIDASE;
COMPND 6 EC: 3.4.14.11;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: PEPX (ORF2);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NCDO 763;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTIL1
KEYWDS ALPHA BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR P.RIGOLET,I.MECHIN,M.M.DELAGE,J.F.CHICH
REVDAT 1 06-NOV-02 1LNS 0
JRNL AUTH P.RIGOLET,I.MECHIN,M.M.DELAGE,J.F.CHICH
JRNL TITL THE STRUCTURAL BASIS FOR CATALYSIS AND SPECIFICITY
JRNL TITL 2 OF THE X-PROLYL DIPEPDIDYL AMINOPEPTIDASE FROM
JRNL TITL 3 LACTOCOCCUS LACTIS
JRNL REF STRUCTURE V. 10 1383 2002
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.500
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 45808
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) : 0.184
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2310
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7179
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 374
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6200
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 308
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.98000
REMARK 3 B22 (A**2) : 1.26000
REMARK 3 B33 (A**2) : -2.24000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.22
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.76
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) : 1.250 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.920 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.160 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.190 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 26.42
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 1LNS COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-2002.
REMARK 100 THE RCSB ID CODE IS RCSB016116.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-1998
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 5.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : DW32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9376
REMARK 200 MONOCHROMATOR : MONOCHROMATOR CRYSTAL SI 111
REMARK 200 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : ROTAVATA-AGROVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46103
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 23.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.8
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: MIR
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 1/2-X,1/2+Y,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 46.25000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.25000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.25000
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 92.50000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 TRP A 469 NE1 TRP A 469 CD1 0.059
REMARK 500 TRP A 469 CE2 TRP A 469 NE1 -0.058
REMARK 500 TRP A 469 CH2 TRP A 469 CZ3 -0.049
REMARK 500 TRP A 504 NE1 TRP A 504 CD1 0.058
REMARK 500 TRP A 504 CE2 TRP A 504 NE1 -0.060
REMARK 500 TRP A 504 CH2 TRP A 504 CZ3 -0.049
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 MET A 132 CG - SD - CE ANGL. DEV. = 9.1 DEGREES
REMARK 500 MET A 205 CG - SD - CE ANGL. DEV. = 9.1 DEGREES
REMARK 500 MET A 344 CG - SD - CE ANGL. DEV. = 9.1 DEGREES
DBREF 1LNS A 1 763 SWS P22346 PEPX_LACLC 1 763
SEQRES 1 A 763 MET ARG PHE ASN HIS PHE SER ILE VAL ASP LYS ASN PHE
SEQRES 2 A 763 ASP GLU GLN LEU ALA GLU LEU ASP GLN LEU GLY PHE ARG
SEQRES 3 A 763 TRP SER VAL PHE TRP ASP GLU LYS LYS ILE LEU LYS ASP
SEQRES 4 A 763 PHE LEU ILE GLN SER PRO SER ASP MET THR ALA LEU GLN
SEQRES 5 A 763 ALA THR ALA GLU LEU ASP VAL ILE GLU PHE LEU LYS SER
SEQRES 6 A 763 SER ILE GLU LEU ASP TRP GLU ILE PHE TRP ASN ILE ALA
SEQRES 7 A 763 LEU GLN LEU LEU ASP PHE VAL PRO ASN PHE ASP PHE GLU
SEQRES 8 A 763 ILE GLY LYS ALA PHE GLU TYR ALA LYS ASN SER ASN LEU
SEQRES 9 A 763 PRO GLN ILE GLU ALA GLU MET THR THR GLU ASN ILE ILE
SEQRES 10 A 763 SER ALA PHE TYR TYR LEU LEU CYS THR ARG ARG LYS THR
SEQRES 11 A 763 GLY MET ILE LEU VAL GLU HIS TRP VAL SER GLU GLY LEU
SEQRES 12 A 763 LEU PRO LEU ASP ASN HIS TYR HIS PHE PHE ASN ASP LYS
SEQRES 13 A 763 SER LEU ALA THR PHE ASP SER SER LEU LEU GLU ARG GLU
SEQRES 14 A 763 VAL LEU TRP VAL GLU SER PRO VAL ASP SER GLU GLN ARG
SEQRES 15 A 763 GLY GLU ASN ASP LEU ILE LYS ILE GLN ILE ILE ARG PRO
SEQRES 16 A 763 LYS SER THR GLU LYS LEU PRO VAL VAL MET THR ALA SER
SEQRES 17 A 763 PRO TYR HIS LEU GLY ILE ASN ASP LYS ALA ASN ASP LEU
SEQRES 18 A 763 ALA LEU HIS ASP MET ASN VAL GLU LEU GLU GLU LYS THR
SEQRES 19 A 763 SER HIS GLU ILE HIS VAL GLU GLN LYS LEU PRO GLN LYS
SEQRES 20 A 763 LEU SER ALA LYS ALA LYS GLU LEU PRO ILE VAL ASP LYS
SEQRES 21 A 763 ALA PRO TYR ARG PHE THR HIS GLY TRP THR TYR SER LEU
SEQRES 22 A 763 ASN ASP TYR PHE LEU THR ARG GLY PHE ALA SER ILE TYR
SEQRES 23 A 763 VAL ALA GLY VAL GLY THR ARG SER SER ASP GLY PHE GLN
SEQRES 24 A 763 THR SER GLY ASP TYR GLN GLN ILE TYR SER MET THR ALA
SEQRES 25 A 763 VAL ILE ASP TRP LEU ASN GLY ARG ALA ARG ALA TYR THR
SEQRES 26 A 763 SER ARG LYS LYS THR HIS GLU ILE LYS ALA SER TRP ALA
SEQRES 27 A 763 ASN GLY LYS VAL ALA MET THR GLY LYS SER TYR LEU GLY
SEQRES 28 A 763 THR MET ALA TYR GLY ALA ALA THR THR GLY VAL GLU GLY
SEQRES 29 A 763 LEU GLU LEU ILE LEU ALA GLU ALA GLY ILE SER SER TRP
SEQRES 30 A 763 TYR ASN TYR TYR ARG GLU ASN GLY LEU VAL ARG SER PRO
SEQRES 31 A 763 GLY GLY PHE PRO GLY GLU ASP LEU ASP VAL LEU ALA ALA
SEQRES 32 A 763 LEU THR TYR SER ARG ASN LEU ASP GLY ALA ASP PHE LEU
SEQRES 33 A 763 LYS GLY ASN ALA GLU TYR GLU LYS ARG LEU ALA GLU MET
SEQRES 34 A 763 THR ALA ALA LEU ASP ARG LYS SER GLY ASP TYR ASN GLN
SEQRES 35 A 763 PHE TRP HIS ASP ARG ASN TYR LEU ILE ASN THR ASP LYS
SEQRES 36 A 763 VAL LYS ALA ASP VAL LEU ILE VAL HIS GLY LEU GLN ASP
SEQRES 37 A 763 TRP ASN VAL THR PRO GLU GLN ALA TYR ASN PHE TRP LYS
SEQRES 38 A 763 ALA LEU PRO GLU GLY HIS ALA LYS HIS ALA PHE LEU HIS
SEQRES 39 A 763 ARG GLY ALA HIS ILE TYR MET ASN SER TRP GLN SER ILE
SEQRES 40 A 763 ASP PHE SER GLU THR ILE ASN ALA TYR PHE VAL ALA LYS
SEQRES 41 A 763 LEU LEU ASP ARG ASP LEU ASN LEU ASN LEU PRO PRO VAL
SEQRES 42 A 763 ILE LEU GLN GLU ASN SER LYS ASP GLN VAL TRP THR MET
SEQRES 43 A 763 MET ASN ASP PHE GLY ALA ASN THR GLN ILE LYS LEU PRO
SEQRES 44 A 763 LEU GLY LYS THR ALA VAL SER PHE ALA GLN PHE ASP ASN
SEQRES 45 A 763 ASN TYR ASP ASP GLU THR PHE LYS LYS TYR SER LYS ASP
SEQRES 46 A 763 PHE ASN VAL PHE LYS LYS ASP LEU PHE GLU ASN LYS ALA
SEQRES 47 A 763 ASN GLU ALA VAL ILE ASP LEU GLU LEU PRO SER MET LEU
SEQRES 48 A 763 THR ILE ASN GLY PRO VAL GLU LEU GLU LEU ARG LEU LYS
SEQRES 49 A 763 LEU ASN ASP THR LYS GLY PHE LEU SER ALA GLN ILE LEU
SEQRES 50 A 763 ASP PHE GLY GLN LYS LYS ARG LEU GLU ASP LYS VAL ARG
SEQRES 51 A 763 VAL LYS ASP PHE LYS VAL LEU ASP ARG GLY ARG ASN PHE
SEQRES 52 A 763 MET LEU ASP ASP LEU VAL GLU LEU PRO LEU VAL GLU SER
SEQRES 53 A 763 PRO TYR GLN LEU VAL THR LYS GLY PHE THR ASN LEU GLN
SEQRES 54 A 763 ASN GLN SER LEU LEU THR VAL SER ASP LEU LYS ALA ASP
SEQRES 55 A 763 GLU TRP PHE THR ILE LYS PHE GLU LEU GLN PRO THR ILE
SEQRES 56 A 763 TYR HIS LEU GLU LYS ALA ASP LYS LEU ARG VAL ILE LEU
SEQRES 57 A 763 TYR SER THR ASP PHE GLU HIS THR VAL ARG ASP ASN ARG
SEQRES 58 A 763 LYS VAL THR TYR GLU ILE ASP LEU SER GLN SER LYS LEU
SEQRES 59 A 763 ILE ILE PRO ILE GLU SER VAL LYS ASN
FORMUL 2 HOH *305(H2 O1)
HELIX 1 1 ASN A 12 LEU A 23 1 12
HELIX 2 2 ASP A 32 GLN A 43 1 12
HELIX 3 3 ASP A 47 LEU A 51 5 5
HELIX 4 4 ASP A 58 SER A 65 1 8
HELIX 5 5 ASP A 70 LEU A 82 1 13
HELIX 6 6 LYS A 94 SER A 102 1 9
HELIX 7 7 THR A 112 THR A 126 1 15
HELIX 8 8 ILE A 133 GLU A 141 1 9
HELIX 9 9 ASP A 162 LEU A 166 5 5
HELIX 10 10 ASN A 215 LEU A 223 1 9
HELIX 11 11 TYR A 271 THR A 279 1 9
HELIX 12 12 ASP A 303 ASN A 318 1 16
HELIX 13 13 SER A 348 THR A 359 1 12
HELIX 14 14 SER A 376 ARG A 382 1 7
HELIX 15 15 ASP A 397 TYR A 406 1 10
HELIX 16 16 SER A 407 LEU A 410 5 4
HELIX 17 17 ASP A 411 ASP A 434 1 24
HELIX 18 18 ASN A 441 ASP A 446 1 6
HELIX 19 19 ARG A 447 VAL A 456 5 10
HELIX 20 20 PRO A 473 LEU A 483 1 11
HELIX 21 21 ASP A 508 LEU A 522 1 15
HELIX 22 22 ASP A 575 ASP A 585 1 11
HELIX 23 23 ASP A 585 GLU A 595 1 11
SHEET 1 A 2 PHE A 152 PHE A 153 0
SHEET 2 A 2 LYS A 156 SER A 157 -1 O LYS A 156 N PHE A 153
SHEET 1 B12 GLU A 332 ILE A 333 0
SHEET 2 B12 ALA A 323 TYR A 324 -1 N ALA A 323 O ILE A 333
SHEET 3 B12 GLU A 167 GLU A 174 -1 N TRP A 172 O TYR A 324
SHEET 4 B12 LEU A 187 ARG A 194 -1 O ILE A 192 N GLU A 169
SHEET 5 B12 ALA A 283 VAL A 287 -1 O SER A 284 N ILE A 193
SHEET 6 B12 LEU A 201 ALA A 207 1 N THR A 206 O ILE A 285
SHEET 7 B12 ALA A 338 LYS A 347 1 O ALA A 343 N MET A 205
SHEET 8 B12 LEU A 365 GLU A 371 1 O LEU A 369 N MET A 344
SHEET 9 B12 ASP A 459 GLY A 465 1 O LEU A 461 N ILE A 368
SHEET 10 B12 LYS A 489 HIS A 494 1 O PHE A 492 N ILE A 462
SHEET 11 B12 VAL A 533 GLN A 536 1 O ILE A 534 N ALA A 491
SHEET 12 B12 TRP A 544 MET A 547 -1 O THR A 545 N LEU A 535
SHEET 1 C 3 HIS A 236 GLU A 237 0
SHEET 2 C 3 THR A 695 VAL A 696 -1 O VAL A 696 N HIS A 236
SHEET 3 C 3 ASN A 690 SER A 692 -1 N SER A 692 O THR A 695
SHEET 1 D 4 PHE A 705 GLU A 710 0
SHEET 2 D 4 GLU A 618 LEU A 625 -1 N LEU A 619 O PHE A 709
SHEET 3 D 4 THR A 744 ASP A 748 -1 O GLU A 746 N LYS A 624
SHEET 4 D 4 PHE A 567 ASP A 571 -1 N ALA A 568 O ILE A 747
SHEET 1 E 4 PHE A 705 GLU A 710 0
SHEET 2 E 4 GLU A 618 LEU A 625 -1 N LEU A 619 O PHE A 709
SHEET 3 E 4 LYS A 753 PRO A 757 -1 O ILE A 755 N GLU A 618
SHEET 4 E 4 GLN A 555 PRO A 559 -1 N LEU A 558 O LEU A 754
SHEET 1 F 4 ALA A 601 GLU A 606 0
SHEET 2 F 4 LYS A 723 TYR A 729 -1 O LEU A 728 N ALA A 601
SHEET 3 F 4 PHE A 631 LEU A 645 -1 N SER A 633 O TYR A 729
SHEET 4 F 4 LEU A 673 ASN A 687 -1 O VAL A 674 N ARG A 644
SHEET 1 G 2 LEU A 611 GLY A 615 0
SHEET 2 G 2 THR A 714 LEU A 718 -1 O LEU A 718 N LEU A 611
SHEET 1 H 2 ARG A 650 LEU A 657 0
SHEET 2 H 2 ASP A 666 GLU A 670 -1 O ASP A 666 N LEU A 657
CRYST1 92.500 102.500 101.500 90.00 90.00 90.00 P 21 21 2 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 0.010811 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009756 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009852 0.00000
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