HEADER HYDROLASE 07-JUN-99 1QQJ
TITLE CRYSTAL STRUCTURE OF MOUSE FUMARYLACETOACETATE HYDROLASE REFINED AT
TITLE 2 1.55 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUMARYLACETOACETATE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETADIKETONASE, FAA;
COMPND 5 EC: 3.7.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS MIXED BETA-SANDWICH ROLL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.TIMM,H.A.MUELLER,P.BHANUMOORTHY,J.M.HARP,G.J.BUNICK
REVDAT 4 14-FEB-24 1QQJ 1 REMARK LINK
REVDAT 3 13-JUL-11 1QQJ 1 VERSN
REVDAT 2 24-FEB-09 1QQJ 1 VERSN
REVDAT 1 07-JUN-00 1QQJ 0
JRNL AUTH D.E.TIMM,H.A.MUELLER,P.BHANUMOORTHY,J.M.HARP,G.J.BUNICK
JRNL TITL CRYSTAL STRUCTURE AND MECHANISM OF A CARBON-CARBON BOND
JRNL TITL 2 HYDROLASE.
JRNL REF STRUCTURE FOLD.DES. V. 7 1023 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10508789
JRNL DOI 10.1016/S0969-2126(99)80170-1
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 3 NUMBER OF REFLECTIONS : 118167
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5952
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6448
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 894
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.10
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.006 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.019 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QQJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000009149.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-97
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.071
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118167
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 29.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 49.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.20400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, SODIUM CACODYLATE, NICKEL
REMARK 280 ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 54.51000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SER A 417
REMARK 465 PRO A 418
REMARK 465 ALA A 419
REMARK 465 SER B 417
REMARK 465 PRO B 418
REMARK 465 ALA B 419
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 126 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 GLU A 199 CG - CD - OE2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 ASP A 233 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 126 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 126 CB - CG - OD2 ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLU B 201 CG - CD - OE2 ANGL. DEV. = -13.8 DEGREES
REMARK 500 GLN B 379 CB - CG - CD ANGL. DEV. = 17.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 16 -84.40 -98.59
REMARK 500 LEU A 17 62.84 64.75
REMARK 500 TYR A 128 47.12 -146.69
REMARK 500 LEU A 195 73.50 -117.90
REMARK 500 PHE A 250 -96.71 -141.56
REMARK 500 TYR A 293 41.57 -155.83
REMARK 500 THR A 382 -64.66 -104.86
REMARK 500 ASN B 16 -82.01 -97.97
REMARK 500 LEU B 17 63.34 64.10
REMARK 500 TYR B 128 45.11 -148.12
REMARK 500 ASN B 146 50.96 -105.94
REMARK 500 PHE B 250 -98.31 -141.45
REMARK 500 TYR B 293 42.14 -157.20
REMARK 500 THR B 382 -61.93 -106.24
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 CA A 420 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 126 OD2
REMARK 620 2 GLU A 199 OE1 170.7
REMARK 620 3 GLU A 201 OE2 96.1 92.6
REMARK 620 4 ASP A 233 OD2 94.2 88.0 97.9
REMARK 620 5 HOH A2068 O 76.5 94.6 172.0 85.9
REMARK 620 6 HOH A2072 O 93.2 82.4 96.1 163.3 81.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 420 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 126 OD2
REMARK 620 2 GLU B 199 OE1 168.3
REMARK 620 3 GLU B 201 OE2 97.7 94.0
REMARK 620 4 ASP B 233 OD2 88.6 89.4 101.9
REMARK 620 5 HOH B2090 O 102.3 77.0 91.1 161.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 2004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QCO RELATED DB: PDB
REMARK 900 RELATED ID: 1QCN RELATED DB: PDB
DBREF 1QQJ A 1 419 UNP P35505 FAAA_MOUSE 1 419
DBREF 1QQJ B 1 419 UNP P35505 FAAA_MOUSE 1 419
SEQRES 1 A 419 MET SER PHE ILE PRO VAL ALA GLU ASP SER ASP PHE PRO
SEQRES 2 A 419 ILE GLN ASN LEU PRO TYR GLY VAL PHE SER THR GLN SER
SEQRES 3 A 419 ASN PRO LYS PRO ARG ILE GLY VAL ALA ILE GLY ASP GLN
SEQRES 4 A 419 ILE LEU ASP LEU SER VAL ILE LYS HIS LEU PHE THR GLY
SEQRES 5 A 419 PRO ALA LEU SER LYS HIS GLN HIS VAL PHE ASP GLU THR
SEQRES 6 A 419 THR LEU ASN ASN PHE MET GLY LEU GLY GLN ALA ALA TRP
SEQRES 7 A 419 LYS GLU ALA ARG ALA SER LEU GLN ASN LEU LEU SER ALA
SEQRES 8 A 419 SER GLN ALA ARG LEU ARG ASP ASP LYS GLU LEU ARG GLN
SEQRES 9 A 419 ARG ALA PHE THR SER GLN ALA SER ALA THR MET HIS LEU
SEQRES 10 A 419 PRO ALA THR ILE GLY ASP TYR THR ASP PHE TYR SER SER
SEQRES 11 A 419 ARG GLN HIS ALA THR ASN VAL GLY ILE MET PHE ARG GLY
SEQRES 12 A 419 LYS GLU ASN ALA LEU LEU PRO ASN TRP LEU HIS LEU PRO
SEQRES 13 A 419 VAL GLY TYR HIS GLY ARG ALA SER SER ILE VAL VAL SER
SEQRES 14 A 419 GLY THR PRO ILE ARG ARG PRO MET GLY GLN MET ARG PRO
SEQRES 15 A 419 ASP ASN SER LYS PRO PRO VAL TYR GLY ALA CYS ARG LEU
SEQRES 16 A 419 LEU ASP MET GLU LEU GLU MET ALA PHE PHE VAL GLY PRO
SEQRES 17 A 419 GLY ASN ARG PHE GLY GLU PRO ILE PRO ILE SER LYS ALA
SEQRES 18 A 419 HIS GLU HIS ILE PHE GLY MET VAL LEU MET ASN ASP TRP
SEQRES 19 A 419 SER ALA ARG ASP ILE GLN GLN TRP GLU TYR VAL PRO LEU
SEQRES 20 A 419 GLY PRO PHE LEU GLY LYS SER PHE GLY THR THR ILE SER
SEQRES 21 A 419 PRO TRP VAL VAL PRO MET ASP ALA LEU MET PRO PHE VAL
SEQRES 22 A 419 VAL PRO ASN PRO LYS GLN ASP PRO LYS PRO LEU PRO TYR
SEQRES 23 A 419 LEU CYS HIS SER GLN PRO TYR THR PHE ASP ILE ASN LEU
SEQRES 24 A 419 SER VAL SER LEU LYS GLY GLU GLY MET SER GLN ALA ALA
SEQRES 25 A 419 THR ILE CYS ARG SER ASN PHE LYS HIS MET TYR TRP THR
SEQRES 26 A 419 MET LEU GLN GLN LEU THR HIS HIS SER VAL ASN GLY CYS
SEQRES 27 A 419 ASN LEU ARG PRO GLY ASP LEU LEU ALA SER GLY THR ILE
SEQRES 28 A 419 SER GLY SER ASP PRO GLU SER PHE GLY SER MET LEU GLU
SEQRES 29 A 419 LEU SER TRP LYS GLY THR LYS ALA ILE ASP VAL GLY GLN
SEQRES 30 A 419 GLY GLN THR ARG THR PHE LEU LEU ASP GLY ASP GLU VAL
SEQRES 31 A 419 ILE ILE THR GLY HIS CYS GLN GLY ASP GLY TYR ARG VAL
SEQRES 32 A 419 GLY PHE GLY GLN CYS ALA GLY LYS VAL LEU PRO ALA LEU
SEQRES 33 A 419 SER PRO ALA
SEQRES 1 B 419 MET SER PHE ILE PRO VAL ALA GLU ASP SER ASP PHE PRO
SEQRES 2 B 419 ILE GLN ASN LEU PRO TYR GLY VAL PHE SER THR GLN SER
SEQRES 3 B 419 ASN PRO LYS PRO ARG ILE GLY VAL ALA ILE GLY ASP GLN
SEQRES 4 B 419 ILE LEU ASP LEU SER VAL ILE LYS HIS LEU PHE THR GLY
SEQRES 5 B 419 PRO ALA LEU SER LYS HIS GLN HIS VAL PHE ASP GLU THR
SEQRES 6 B 419 THR LEU ASN ASN PHE MET GLY LEU GLY GLN ALA ALA TRP
SEQRES 7 B 419 LYS GLU ALA ARG ALA SER LEU GLN ASN LEU LEU SER ALA
SEQRES 8 B 419 SER GLN ALA ARG LEU ARG ASP ASP LYS GLU LEU ARG GLN
SEQRES 9 B 419 ARG ALA PHE THR SER GLN ALA SER ALA THR MET HIS LEU
SEQRES 10 B 419 PRO ALA THR ILE GLY ASP TYR THR ASP PHE TYR SER SER
SEQRES 11 B 419 ARG GLN HIS ALA THR ASN VAL GLY ILE MET PHE ARG GLY
SEQRES 12 B 419 LYS GLU ASN ALA LEU LEU PRO ASN TRP LEU HIS LEU PRO
SEQRES 13 B 419 VAL GLY TYR HIS GLY ARG ALA SER SER ILE VAL VAL SER
SEQRES 14 B 419 GLY THR PRO ILE ARG ARG PRO MET GLY GLN MET ARG PRO
SEQRES 15 B 419 ASP ASN SER LYS PRO PRO VAL TYR GLY ALA CYS ARG LEU
SEQRES 16 B 419 LEU ASP MET GLU LEU GLU MET ALA PHE PHE VAL GLY PRO
SEQRES 17 B 419 GLY ASN ARG PHE GLY GLU PRO ILE PRO ILE SER LYS ALA
SEQRES 18 B 419 HIS GLU HIS ILE PHE GLY MET VAL LEU MET ASN ASP TRP
SEQRES 19 B 419 SER ALA ARG ASP ILE GLN GLN TRP GLU TYR VAL PRO LEU
SEQRES 20 B 419 GLY PRO PHE LEU GLY LYS SER PHE GLY THR THR ILE SER
SEQRES 21 B 419 PRO TRP VAL VAL PRO MET ASP ALA LEU MET PRO PHE VAL
SEQRES 22 B 419 VAL PRO ASN PRO LYS GLN ASP PRO LYS PRO LEU PRO TYR
SEQRES 23 B 419 LEU CYS HIS SER GLN PRO TYR THR PHE ASP ILE ASN LEU
SEQRES 24 B 419 SER VAL SER LEU LYS GLY GLU GLY MET SER GLN ALA ALA
SEQRES 25 B 419 THR ILE CYS ARG SER ASN PHE LYS HIS MET TYR TRP THR
SEQRES 26 B 419 MET LEU GLN GLN LEU THR HIS HIS SER VAL ASN GLY CYS
SEQRES 27 B 419 ASN LEU ARG PRO GLY ASP LEU LEU ALA SER GLY THR ILE
SEQRES 28 B 419 SER GLY SER ASP PRO GLU SER PHE GLY SER MET LEU GLU
SEQRES 29 B 419 LEU SER TRP LYS GLY THR LYS ALA ILE ASP VAL GLY GLN
SEQRES 30 B 419 GLY GLN THR ARG THR PHE LEU LEU ASP GLY ASP GLU VAL
SEQRES 31 B 419 ILE ILE THR GLY HIS CYS GLN GLY ASP GLY TYR ARG VAL
SEQRES 32 B 419 GLY PHE GLY GLN CYS ALA GLY LYS VAL LEU PRO ALA LEU
SEQRES 33 B 419 SER PRO ALA
HET CA A 420 1
HET ACT A2001 4
HET CAC A2004 5
HET CA B 420 1
HET ACT B2000 4
HET CAC B2003 5
HETNAM CA CALCIUM ION
HETNAM ACT ACETATE ION
HETNAM CAC CACODYLATE ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 3 CA 2(CA 2+)
FORMUL 4 ACT 2(C2 H3 O2 1-)
FORMUL 5 CAC 2(C2 H6 AS O2 1-)
FORMUL 9 HOH *894(H2 O)
HELIX 1 1 LEU A 43 LYS A 47 1 5
HELIX 2 2 HIS A 48 PHE A 50 5 3
HELIX 3 3 HIS A 58 GLU A 64 5 7
HELIX 4 4 LEU A 67 LEU A 73 1 7
HELIX 5 5 GLY A 74 SER A 90 1 17
HELIX 6 6 ASP A 99 ALA A 106 1 8
HELIX 7 7 ALA A 111 ALA A 113 5 3
HELIX 8 8 SER A 130 GLY A 143 1 14
HELIX 9 9 LYS A 144 ALA A 147 5 4
HELIX 10 10 PRO A 217 HIS A 222 1 6
HELIX 11 11 ARG A 237 TYR A 244 1 8
HELIX 12 12 PHE A 250 PHE A 255 1 6
HELIX 13 13 MET A 266 MET A 270 1 5
HELIX 14 14 LEU A 284 CYS A 288 5 5
HELIX 15 15 THR A 325 VAL A 335 1 11
HELIX 16 16 ASP A 355 PHE A 359 5 5
HELIX 17 17 SER A 361 SER A 366 1 6
HELIX 18 18 LEU B 43 LYS B 47 1 5
HELIX 19 19 HIS B 48 PHE B 50 5 3
HELIX 20 20 HIS B 58 GLU B 64 5 7
HELIX 21 21 LEU B 67 LEU B 73 1 7
HELIX 22 22 GLY B 74 LEU B 89 1 16
HELIX 23 23 ASP B 99 ALA B 106 1 8
HELIX 24 24 SER B 130 GLY B 143 1 14
HELIX 25 25 LYS B 144 ALA B 147 5 4
HELIX 26 26 PRO B 217 HIS B 222 1 6
HELIX 27 27 ARG B 237 TYR B 244 1 8
HELIX 28 28 PHE B 250 PHE B 255 1 6
HELIX 29 29 MET B 266 MET B 270 1 5
HELIX 30 30 LEU B 284 CYS B 288 5 5
HELIX 31 31 LYS B 320 MET B 322 5 3
HELIX 32 32 THR B 325 VAL B 335 1 11
HELIX 33 33 ASP B 355 PHE B 359 5 5
HELIX 34 34 SER B 361 SER B 366 1 6
SHEET 1 A 5 PHE A 107 SER A 109 0
SHEET 2 A 5 GLN A 39 ASP A 42 -1 N ILE A 40 O THR A 108
SHEET 3 A 5 ARG A 31 ILE A 36 -1 O VAL A 34 N LEU A 41
SHEET 4 A 5 TYR A 19 SER A 23 -1 O GLY A 20 N GLY A 33
SHEET 5 A 5 THR A 114 HIS A 116 -1 N THR A 114 O SER A 23
SHEET 1 B 7 GLY A 158 HIS A 160 0
SHEET 2 B 7 TYR A 124 PHE A 127 -1 N ASP A 126 O TYR A 159
SHEET 3 B 7 LEU A 345 ALA A 347 1 O LEU A 345 N THR A 125
SHEET 4 B 7 LEU A 200 VAL A 206 -1 N PHE A 204 O LEU A 346
SHEET 5 B 7 ILE A 225 ASN A 232 -1 N PHE A 226 O PHE A 205
SHEET 6 B 7 THR A 257 ILE A 259 -1 O THR A 258 N ASN A 232
SHEET 7 B 7 ILE A 166 VAL A 168 1 N VAL A 167 O THR A 257
SHEET 1 B1 6 GLY A 158 HIS A 160 0
SHEET 2 B1 6 TYR A 124 PHE A 127 -1 N ASP A 126 O TYR A 159
SHEET 3 B1 6 LEU A 345 ALA A 347 1 O LEU A 345 N THR A 125
SHEET 4 B1 6 LEU A 200 VAL A 206 -1 N PHE A 204 O LEU A 346
SHEET 5 B1 6 ILE A 225 ASN A 232 -1 N PHE A 226 O PHE A 205
SHEET 6 B1 6 VAL A 264 PRO A 265 -1 O VAL A 264 N MET A 228
SHEET 1 C 5 ILE A 173 ARG A 174 0
SHEET 2 C 5 ARG A 402 LEU A 413 1 O LYS A 411 N ILE A 173
SHEET 3 C 5 GLU A 389 GLN A 397 -1 N VAL A 390 O GLY A 410
SHEET 4 C 5 ASN A 298 LYS A 304 -1 N ASN A 298 O HIS A 395
SHEET 5 C 5 ALA A 312 ASN A 318 -1 N ALA A 312 O LEU A 303
SHEET 1 D 2 MET A 177 MET A 180 0
SHEET 2 D 2 VAL A 189 ALA A 192 -1 N VAL A 189 O MET A 180
SHEET 1 E 2 LEU A 196 ASP A 197 0
SHEET 2 E 2 SER A 235 ALA A 236 -1 O SER A 235 N ASP A 197
SHEET 1 F 2 VAL A 273 VAL A 274 0
SHEET 2 F 2 THR A 294 PHE A 295 -1 O THR A 294 N VAL A 274
SHEET 1 G 2 ILE A 373 ASP A 374 0
SHEET 2 G 2 THR A 380 ARG A 381 -1 O ARG A 381 N ILE A 373
SHEET 1 H 5 PHE B 107 SER B 109 0
SHEET 2 H 5 GLN B 39 ASP B 42 -1 N ILE B 40 O THR B 108
SHEET 3 H 5 ASN B 27 ILE B 36 -1 O VAL B 34 N LEU B 41
SHEET 4 H 5 TYR B 19 THR B 24 -1 O GLY B 20 N GLY B 33
SHEET 5 H 5 ALA B 113 HIS B 116 -1 N THR B 114 O SER B 23
SHEET 1 I 7 GLY B 158 HIS B 160 0
SHEET 2 I 7 TYR B 124 PHE B 127 -1 N ASP B 126 O TYR B 159
SHEET 3 I 7 LEU B 345 ALA B 347 1 O LEU B 345 N THR B 125
SHEET 4 I 7 LEU B 200 VAL B 206 -1 O PHE B 204 N LEU B 346
SHEET 5 I 7 ILE B 225 ASN B 232 -1 N PHE B 226 O PHE B 205
SHEET 6 I 7 THR B 257 ILE B 259 -1 O THR B 258 N ASN B 232
SHEET 7 I 7 ILE B 166 VAL B 168 1 N VAL B 167 O THR B 257
SHEET 1 I1 6 GLY B 158 HIS B 160 0
SHEET 2 I1 6 TYR B 124 PHE B 127 -1 N ASP B 126 O TYR B 159
SHEET 3 I1 6 LEU B 345 ALA B 347 1 O LEU B 345 N THR B 125
SHEET 4 I1 6 LEU B 200 VAL B 206 -1 O PHE B 204 N LEU B 346
SHEET 5 I1 6 ILE B 225 ASN B 232 -1 N PHE B 226 O PHE B 205
SHEET 6 I1 6 VAL B 264 PRO B 265 -1 O VAL B 264 N MET B 228
SHEET 1 J 4 ALA B 312 ASN B 318 0
SHEET 2 J 4 ASN B 298 LYS B 304 -1 N LEU B 299 O SER B 317
SHEET 3 J 4 GLU B 389 GLN B 397 -1 N GLU B 389 O LYS B 304
SHEET 4 J 4 ARG B 402 GLY B 404 -1 O VAL B 403 N CYS B 396
SHEET 1 J1 5 ALA B 312 ASN B 318 0
SHEET 2 J1 5 ASN B 298 LYS B 304 -1 N LEU B 299 O SER B 317
SHEET 3 J1 5 GLU B 389 GLN B 397 -1 N GLU B 389 O LYS B 304
SHEET 4 J1 5 CYS B 408 LEU B 413 -1 O CYS B 408 N ILE B 392
SHEET 5 J1 5 ILE B 173 ARG B 174 1 N ILE B 173 O LYS B 411
SHEET 1 K 2 MET B 177 MET B 180 0
SHEET 2 K 2 VAL B 189 ALA B 192 -1 N VAL B 189 O MET B 180
SHEET 1 L 2 LEU B 196 ASP B 197 0
SHEET 2 L 2 SER B 235 ALA B 236 -1 O SER B 235 N ASP B 197
SHEET 1 M 2 VAL B 273 VAL B 274 0
SHEET 2 M 2 THR B 294 PHE B 295 -1 O THR B 294 N VAL B 274
SHEET 1 N 2 ILE B 373 ASP B 374 0
SHEET 2 N 2 THR B 380 ARG B 381 -1 O ARG B 381 N ILE B 373
LINK OD2 ASP A 126 CA CA A 420 1555 1555 2.64
LINK OE1 GLU A 199 CA CA A 420 1555 1555 2.61
LINK OE2 GLU A 201 CA CA A 420 1555 1555 2.62
LINK OD2 ASP A 233 CA CA A 420 1555 1555 2.69
LINK CA CA A 420 O HOH A2068 1555 1555 3.01
LINK CA CA A 420 O HOH A2072 1555 1555 2.87
LINK OD2 ASP B 126 CA CA B 420 1555 1555 2.63
LINK OE1 GLU B 199 CA CA B 420 1555 1555 2.65
LINK OE2 GLU B 201 CA CA B 420 1555 1555 2.63
LINK OD2 ASP B 233 CA CA B 420 1555 1555 2.72
LINK CA CA B 420 O HOH B2090 1555 1555 3.07
CISPEP 1 VAL A 245 PRO A 246 0 8.68
CISPEP 2 ASP A 280 PRO A 281 0 8.55
CISPEP 3 VAL B 245 PRO B 246 0 10.05
CISPEP 4 ASP B 280 PRO B 281 0 6.47
SITE 1 AC1 5 ASP B 126 GLU B 199 GLU B 201 ASP B 233
SITE 2 AC1 5 HOH B2090
SITE 1 AC2 7 ASP A 126 GLU A 199 GLU A 201 ASP A 233
SITE 2 AC2 7 LYS A 253 HOH A2068 HOH A2072
SITE 1 AC3 6 PRO A 246 TYR B 128 VAL B 137 ARG B 142
SITE 2 AC3 6 HOH B2054 HOH B2061
SITE 1 AC4 7 TYR A 128 VAL A 137 ARG A 142 CAC A2004
SITE 2 AC4 7 HOH A2032 HOH A2033 PRO B 246
SITE 1 AC5 7 TYR B 128 HIS B 133 GLU B 199 ARG B 237
SITE 2 AC5 7 GLN B 240 LYS B 253 HOH B2090
SITE 1 AC6 12 TYR A 128 HIS A 133 VAL A 137 GLU A 199
SITE 2 AC6 12 ARG A 237 GLN A 240 LYS A 253 THR A 350
SITE 3 AC6 12 ACT A2001 HOH A2068 HOH A2072 LEU B 247
CRYST1 64.000 109.020 65.240 90.00 95.68 90.00 P 1 21 1 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 0.015625 0.000000 0.001554 0.00000
SCALE2 0.000000 0.009173 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015404 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
