HEADER HYDROLASE 12-MAR-99 5BCA
TITLE BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (1,4-ALPHA-D-GLUCAN MALTOHYDROLASE.);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.2.1.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE 3 ORGANISM_TAXID: 1396;
SOURCE 4 STRAIN: BACILLUS CEREUS;
SOURCE 5 VARIANT: MYCOIDES;
SOURCE 6 CELLULAR_LOCATION: EXTRACELLULAR
KEYWDS HYDROLASE, BETA-AMYLASE, RAW-STARCH BINDING DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.OYAMA,M.KUSUNOKI,Y.KISHIMOTO,Y.TAKASAKI,Y.NITTA
REVDAT 3 27-DEC-23 5BCA 1 REMARK LINK
REVDAT 2 24-FEB-09 5BCA 1 VERSN
REVDAT 1 15-MAR-00 5BCA 0
JRNL AUTH T.OYAMA,M.KUSUNOKI,Y.KISHIMOTO,Y.TAKASAKI,Y.NITTA
JRNL TITL CRYSTAL STRUCTURE OF BETA-AMYLASE FROM BACILLUS CEREUS VAR.
JRNL TITL 2 MYCOIDES AT 2.2 A RESOLUTION.
JRNL REF J.BIOCHEM.(TOKYO) V. 125 1120 1999
JRNL REFN ISSN 0021-924X
JRNL PMID 10348915
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.OYAMA,M.KUSUNOKI,Y.KISHIMOTO,Y.TAKASAKI,Y.NITTA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK 1 TITL 2 BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES
REMARK 1 REF PROTEIN PEPT.LETT. V. 5 349 1998
REMARK 1 REFN ISSN 0929-8665
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.NITTA,M.SHIRAKAWA,Y.TAKASAKI
REMARK 1 TITL KINETIC STUDY OF ACTIVE SITE STRUCTURE OF BETA-AMYLASE FROM
REMARK 1 TITL 2 BACILLUS CEREUS VAR. MYCOIDES
REMARK 1 REF BIOSCI.BIOTECHNOL.BIOCHEM. V. 60 823 1996
REMARK 1 REFN ISSN 0916-8451
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.YAMAGUCHI,Y.MATSUMOTO,M.SHIRAKAWA,M.KIBE,T.HIBINO,
REMARK 1 AUTH 2 S.KOZAKI,Y.TAKASAKI,Y.NITTA
REMARK 1 TITL CLONING, SEQUENCING, AND EXPRESSION OF A BETA-AMYLASE GENE
REMARK 1 TITL 2 FROM BACILLUS CEREUS VAR. MYCOIDES AND CHARACTERIZATION OF
REMARK 1 TITL 3 ITS PRODUCTS
REMARK 1 REF BIOSCI.BIOTECHNOL.BIOCHEM. V. 60 1255 1996
REMARK 1 REFN ISSN 0916-8451
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 74.0
REMARK 3 NUMBER OF REFLECTIONS : 102087
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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16476
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 752
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.97
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): 0.250
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) : 0.014 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.039 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.041 ; 0.050
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) : 0.135 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.194 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.219 ; 0.300
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) : 4.500 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 20.700; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 31.000; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.706 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.570 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.096 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.136 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5BCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000642.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : PHOTON FACTORY
REMARK 200 OPTICS : BENT QUARTZ CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : WEISSENBERG IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : PHOTON FACTORY
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113923
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 95.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.5
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
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) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.20800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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 (%): 59.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 9.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 88.95000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 88.95000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 56.45000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP B 489 OG1 THR B 491 1.84
REMARK 500 NZ LYS B 21 OD2 ASP B 54 1.96
REMARK 500 OH TYR C 164 OG1 THR C 328 1.99
REMARK 500 OH TYR A 460 OD1 ASN A 465 2.01
REMARK 500 OH TYR A 211 OD2 ASP A 252 2.03
REMARK 500 N ILE C 284 O HOH C 639 2.13
REMARK 500 OD2 ASP C 49 O HOH C 722 2.13
REMARK 500 OE2 GLU A 216 NZ LYS A 219 2.14
REMARK 500 OE1 GLU D 305 O HOH D 644 2.15
REMARK 500 OG SER B 487 OD2 ASP B 489 2.15
REMARK 500 OD2 ASP D 336 OG1 THR D 348 2.16
REMARK 500 O ASP D 182 NZ LYS D 191 2.17
REMARK 500 OD1 ASN C 374 N GLU C 376 2.18
REMARK 500 NZ LYS C 200 O HOH C 773 2.18
REMARK 500 OH TYR C 67 O HOH C 651 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 10 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 34 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP A 60 CB - CG - OD2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 CYS A 91 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 114 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TYR A 117 CB - CA - C ANGL. DEV. = 12.6 DEGREES
REMARK 500 ASP A 136 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 139 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP A 252 CB - CG - OD1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 GLU A 305 OE1 - CD - OE2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TYR A 310 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TYR A 310 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ASP A 326 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 380 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 380 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 397 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP A 413 CB - CG - OD1 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASP A 413 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 443 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TYR A 454 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 TYR A 454 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 GLU A 480 OE1 - CD - OE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TYR B 14 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG B 36 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG B 36 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP B 97 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP B 98 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP B 114 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG B 139 CD - NE - CZ ANGL. DEV. = 14.4 DEGREES
REMARK 500 ARG B 139 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ASP B 158 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 SER B 166 CA - C - O ANGL. DEV. = -12.9 DEGREES
REMARK 500 ARG B 174 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 189 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP B 236 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 236 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR B 257 CB - CG - CD2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 TYR B 257 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TYR B 310 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR B 310 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP B 312 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP B 318 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASN B 352 N - CA - CB ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG B 380 CD - NE - CZ ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG B 380 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 380 NE - CZ - NH2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 ASP B 413 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 443 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 118 ANGLE DEVIATIONS.
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 THR A 26 -133.89 -147.96
REMARK 500 GLU A 56 38.52 -144.40
REMARK 500 GLN A 62 76.51 -101.27
REMARK 500 ASP A 64 88.32 -155.52
REMARK 500 THR A 88 21.93 -77.99
REMARK 500 ASN A 100 89.16 -162.42
REMARK 500 ASP A 113 -168.44 -100.75
REMARK 500 ASN A 243 -14.96 -155.21
REMARK 500 LYS A 337 -64.82 -124.82
REMARK 500 TYR A 398 -74.85 -14.34
REMARK 500 ASN A 465 73.65 54.34
REMARK 500 LYS A 488 -32.23 -37.97
REMARK 500 SER A 494 163.52 178.31
REMARK 500 THR A 510 -168.18 -165.28
REMARK 500 THR B 26 -157.00 -154.87
REMARK 500 ALA B 170 19.19 57.91
REMARK 500 ASN B 243 -17.26 -155.21
REMARK 500 CYS B 331 32.52 83.28
REMARK 500 LYS B 337 -70.67 -116.62
REMARK 500 ASN B 428 40.78 88.27
REMARK 500 TRP B 449 13.93 49.60
REMARK 500 SER B 501 142.82 -177.74
REMARK 500 THR B 510 -152.11 -137.41
REMARK 500 THR C 26 -158.40 -168.98
REMARK 500 THR C 88 34.07 -89.54
REMARK 500 VAL C 95 129.81 -35.45
REMARK 500 ASN C 100 87.27 -160.17
REMARK 500 ALA C 170 11.49 48.67
REMARK 500 ARG C 174 -177.37 -171.18
REMARK 500 ASN C 243 -2.25 -156.69
REMARK 500 GLN C 294 18.24 56.02
REMARK 500 ILE C 300 72.05 -119.01
REMARK 500 TYR C 398 -67.08 -25.27
REMARK 500 TRP C 449 -1.68 73.97
REMARK 500 LYS C 488 -62.78 -27.24
REMARK 500 ASP C 489 -1.13 -48.37
REMARK 500 THR C 510 -151.43 -160.54
REMARK 500 THR D 26 -135.83 -151.26
REMARK 500 GLU D 56 43.86 -144.27
REMARK 500 VAL D 95 118.17 -38.69
REMARK 500 TYR D 117 -165.26 -122.73
REMARK 500 THR D 129 155.23 173.77
REMARK 500 PRO D 132 -6.10 -52.02
REMARK 500 LYS D 140 -71.72 -65.23
REMARK 500 PRO D 187 33.97 -98.08
REMARK 500 GLN D 193 59.97 -117.81
REMARK 500 ALA D 194 50.44 -144.16
REMARK 500 LYS D 219 -84.30 -53.81
REMARK 500 LEU D 229 1.11 -62.53
REMARK 500 ASN D 243 -14.10 -153.23
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 72 10.83
REMARK 500 ALA B 134 10.68
REMARK 500 PHE B 276 12.14
REMARK 500 ALA C 220 12.06
REMARK 500 PHE D 50 11.34
REMARK 500 TYR D 146 14.85
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 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 56 OE2
REMARK 620 2 ASP A 60 OD1 94.0
REMARK 620 3 GLN A 61 OE1 92.4 100.7
REMARK 620 4 GLU A 141 OE1 113.2 94.2 149.4
REMARK 620 5 GLU A 144 OE1 157.0 103.0 69.4 81.3
REMARK 620 6 HOH A 602 O 65.1 148.5 103.4 74.9 104.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 602 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 56 OE2
REMARK 620 2 ASP B 60 OD1 92.0
REMARK 620 3 GLN B 61 OE1 94.2 86.0
REMARK 620 4 GLU B 141 OE1 107.6 91.1 158.0
REMARK 620 5 GLU B 144 OE1 167.8 86.8 73.6 84.5
REMARK 620 6 HOH B 603 O 74.7 164.2 103.1 85.2 108.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 603 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 56 OE2
REMARK 620 2 ASP C 60 OD1 89.6
REMARK 620 3 GLN C 61 OE1 94.9 95.0
REMARK 620 4 GLU C 141 OE1 114.5 88.5 150.4
REMARK 620 5 GLU C 144 OE1 167.2 90.3 72.3 78.3
REMARK 620 6 HOH C 604 O 78.0 163.6 96.7 86.9 104.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 56 OE2
REMARK 620 2 ASP D 60 OD1 83.3
REMARK 620 3 GLN D 61 OE1 93.0 94.8
REMARK 620 4 GLU D 141 OE1 110.8 88.0 156.2
REMARK 620 5 GLU D 144 OE1 166.1 95.4 73.3 82.9
REMARK 620 6 HOH D 605 O 71.5 149.2 103.7 84.9 113.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAC
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAD
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 604
DBREF 5BCA A 1 516 UNP Q9Z4N9 Q9Z4N9_BACCE 31 546
DBREF 5BCA B 1 516 UNP Q9Z4N9 Q9Z4N9_BACCE 31 546
DBREF 5BCA C 1 516 UNP Q9Z4N9 Q9Z4N9_BACCE 31 546
DBREF 5BCA D 1 516 UNP Q9Z4N9 Q9Z4N9_BACCE 31 546
SEQRES 1 A 516 ALA VAL ASN GLY LYS GLY MET ASN PRO ASP TYR LYS ALA
SEQRES 2 A 516 TYR LEU MET ALA PRO LEU LYS LYS ILE PRO GLU VAL THR
SEQRES 3 A 516 ASN TRP GLU THR PHE GLU ASN ASP LEU ARG TRP ALA LYS
SEQRES 4 A 516 GLN ASN GLY PHE TYR ALA ILE THR VAL ASP PHE TRP TRP
SEQRES 5 A 516 GLY ASP MET GLU LYS ASN GLY ASP GLN GLN PHE ASP PHE
SEQRES 6 A 516 SER TYR ALA GLN ARG PHE ALA GLN SER VAL LYS ASN ALA
SEQRES 7 A 516 GLY MET LYS MET ILE PRO ILE ILE SER THR HIS GLN CYS
SEQRES 8 A 516 GLY GLY ASN VAL GLY ASP ASP CYS ASN VAL PRO ILE PRO
SEQRES 9 A 516 SER TRP VAL TRP ASN GLN LYS SER ASP ASP SER LEU TYR
SEQRES 10 A 516 PHE LYS SER GLU THR GLY THR VAL ASN LYS GLU THR LEU
SEQRES 11 A 516 ASN PRO LEU ALA SER ASP VAL ILE ARG LYS GLU TYR GLY
SEQRES 12 A 516 GLU LEU TYR THR ALA PHE ALA ALA ALA MET LYS PRO TYR
SEQRES 13 A 516 LYS ASP VAL ILE ALA LYS ILE TYR LEU SER GLY GLY PRO
SEQRES 14 A 516 ALA GLY GLU LEU ARG TYR PRO SER TYR THR THR SER ASP
SEQRES 15 A 516 GLY THR GLY TYR PRO SER ARG GLY LYS PHE GLN ALA TYR
SEQRES 16 A 516 THR GLU PHE ALA LYS SER LYS PHE ARG LEU TRP VAL LEU
SEQRES 17 A 516 ASN LYS TYR GLY SER LEU ASN GLU VAL ASN LYS ALA TRP
SEQRES 18 A 516 GLY THR LYS LEU ILE SER GLU LEU ALA ILE LEU PRO PRO
SEQRES 19 A 516 SER ASP GLY GLU GLN PHE LEU MET ASN GLY TYR LEU SER
SEQRES 20 A 516 MET TYR GLY LYS ASP TYR LEU GLU TRP TYR GLN GLY ILE
SEQRES 21 A 516 LEU GLU ASN HIS THR LYS LEU ILE GLY GLU LEU ALA HIS
SEQRES 22 A 516 ASN ALA PHE ASP THR THR PHE GLN VAL PRO ILE GLY ALA
SEQRES 23 A 516 LYS ILE ALA GLY VAL HIS TRP GLN TYR ASN ASN PRO THR
SEQRES 24 A 516 ILE PRO HIS GLY ALA GLU LYS PRO ALA GLY TYR ASN ASP
SEQRES 25 A 516 TYR SER HIS LEU LEU ASP ALA PHE LYS SER ALA LYS LEU
SEQRES 26 A 516 ASP VAL THR PHE THR CYS LEU GLU MET THR ASP LYS GLY
SEQRES 27 A 516 SER TYR PRO GLU TYR SER MET PRO LYS THR LEU VAL GLN
SEQRES 28 A 516 ASN ILE ALA THR LEU ALA ASN GLU LYS GLY ILE VAL LEU
SEQRES 29 A 516 ASN GLY GLU ASN ALA LEU SER ILE GLY ASN GLU GLU GLU
SEQRES 30 A 516 TYR LYS ARG VAL ALA GLU MET ALA PHE ASN TYR ASN PHE
SEQRES 31 A 516 ALA GLY PHE THR LEU LEU ARG TYR GLN ASP VAL MET TYR
SEQRES 32 A 516 ASN ASN SER LEU MET GLY LYS PHE LYS ASP LEU LEU GLY
SEQRES 33 A 516 VAL THR PRO VAL MET GLN THR ILE VAL VAL LYS ASN VAL
SEQRES 34 A 516 PRO THR THR ILE GLY ASP THR VAL TYR ILE THR GLY ASN
SEQRES 35 A 516 ARG ALA GLU LEU GLY SER TRP ASP THR LYS GLN TYR PRO
SEQRES 36 A 516 ILE GLN LEU TYR TYR ASP SER HIS SER ASN ASP TRP ARG
SEQRES 37 A 516 GLY ASN VAL VAL LEU PRO ALA GLU ARG ASN ILE GLU PHE
SEQRES 38 A 516 LYS ALA PHE ILE LYS SER LYS ASP GLY THR VAL LYS SER
SEQRES 39 A 516 TRP GLN THR ILE GLN GLN SER TRP ASN PRO VAL PRO LEU
SEQRES 40 A 516 LYS THR THR SER HIS THR SER SER TRP
SEQRES 1 B 516 ALA VAL ASN GLY LYS GLY MET ASN PRO ASP TYR LYS ALA
SEQRES 2 B 516 TYR LEU MET ALA PRO LEU LYS LYS ILE PRO GLU VAL THR
SEQRES 3 B 516 ASN TRP GLU THR PHE GLU ASN ASP LEU ARG TRP ALA LYS
SEQRES 4 B 516 GLN ASN GLY PHE TYR ALA ILE THR VAL ASP PHE TRP TRP
SEQRES 5 B 516 GLY ASP MET GLU LYS ASN GLY ASP GLN GLN PHE ASP PHE
SEQRES 6 B 516 SER TYR ALA GLN ARG PHE ALA GLN SER VAL LYS ASN ALA
SEQRES 7 B 516 GLY MET LYS MET ILE PRO ILE ILE SER THR HIS GLN CYS
SEQRES 8 B 516 GLY GLY ASN VAL GLY ASP ASP CYS ASN VAL PRO ILE PRO
SEQRES 9 B 516 SER TRP VAL TRP ASN GLN LYS SER ASP ASP SER LEU TYR
SEQRES 10 B 516 PHE LYS SER GLU THR GLY THR VAL ASN LYS GLU THR LEU
SEQRES 11 B 516 ASN PRO LEU ALA SER ASP VAL ILE ARG LYS GLU TYR GLY
SEQRES 12 B 516 GLU LEU TYR THR ALA PHE ALA ALA ALA MET LYS PRO TYR
SEQRES 13 B 516 LYS ASP VAL ILE ALA LYS ILE TYR LEU SER GLY GLY PRO
SEQRES 14 B 516 ALA GLY GLU LEU ARG TYR PRO SER TYR THR THR SER ASP
SEQRES 15 B 516 GLY THR GLY TYR PRO SER ARG GLY LYS PHE GLN ALA TYR
SEQRES 16 B 516 THR GLU PHE ALA LYS SER LYS PHE ARG LEU TRP VAL LEU
SEQRES 17 B 516 ASN LYS TYR GLY SER LEU ASN GLU VAL ASN LYS ALA TRP
SEQRES 18 B 516 GLY THR LYS LEU ILE SER GLU LEU ALA ILE LEU PRO PRO
SEQRES 19 B 516 SER ASP GLY GLU GLN PHE LEU MET ASN GLY TYR LEU SER
SEQRES 20 B 516 MET TYR GLY LYS ASP TYR LEU GLU TRP TYR GLN GLY ILE
SEQRES 21 B 516 LEU GLU ASN HIS THR LYS LEU ILE GLY GLU LEU ALA HIS
SEQRES 22 B 516 ASN ALA PHE ASP THR THR PHE GLN VAL PRO ILE GLY ALA
SEQRES 23 B 516 LYS ILE ALA GLY VAL HIS TRP GLN TYR ASN ASN PRO THR
SEQRES 24 B 516 ILE PRO HIS GLY ALA GLU LYS PRO ALA GLY TYR ASN ASP
SEQRES 25 B 516 TYR SER HIS LEU LEU ASP ALA PHE LYS SER ALA LYS LEU
SEQRES 26 B 516 ASP VAL THR PHE THR CYS LEU GLU MET THR ASP LYS GLY
SEQRES 27 B 516 SER TYR PRO GLU TYR SER MET PRO LYS THR LEU VAL GLN
SEQRES 28 B 516 ASN ILE ALA THR LEU ALA ASN GLU LYS GLY ILE VAL LEU
SEQRES 29 B 516 ASN GLY GLU ASN ALA LEU SER ILE GLY ASN GLU GLU GLU
SEQRES 30 B 516 TYR LYS ARG VAL ALA GLU MET ALA PHE ASN TYR ASN PHE
SEQRES 31 B 516 ALA GLY PHE THR LEU LEU ARG TYR GLN ASP VAL MET TYR
SEQRES 32 B 516 ASN ASN SER LEU MET GLY LYS PHE LYS ASP LEU LEU GLY
SEQRES 33 B 516 VAL THR PRO VAL MET GLN THR ILE VAL VAL LYS ASN VAL
SEQRES 34 B 516 PRO THR THR ILE GLY ASP THR VAL TYR ILE THR GLY ASN
SEQRES 35 B 516 ARG ALA GLU LEU GLY SER TRP ASP THR LYS GLN TYR PRO
SEQRES 36 B 516 ILE GLN LEU TYR TYR ASP SER HIS SER ASN ASP TRP ARG
SEQRES 37 B 516 GLY ASN VAL VAL LEU PRO ALA GLU ARG ASN ILE GLU PHE
SEQRES 38 B 516 LYS ALA PHE ILE LYS SER LYS ASP GLY THR VAL LYS SER
SEQRES 39 B 516 TRP GLN THR ILE GLN GLN SER TRP ASN PRO VAL PRO LEU
SEQRES 40 B 516 LYS THR THR SER HIS THR SER SER TRP
SEQRES 1 C 516 ALA VAL ASN GLY LYS GLY MET ASN PRO ASP TYR LYS ALA
SEQRES 2 C 516 TYR LEU MET ALA PRO LEU LYS LYS ILE PRO GLU VAL THR
SEQRES 3 C 516 ASN TRP GLU THR PHE GLU ASN ASP LEU ARG TRP ALA LYS
SEQRES 4 C 516 GLN ASN GLY PHE TYR ALA ILE THR VAL ASP PHE TRP TRP
SEQRES 5 C 516 GLY ASP MET GLU LYS ASN GLY ASP GLN GLN PHE ASP PHE
SEQRES 6 C 516 SER TYR ALA GLN ARG PHE ALA GLN SER VAL LYS ASN ALA
SEQRES 7 C 516 GLY MET LYS MET ILE PRO ILE ILE SER THR HIS GLN CYS
SEQRES 8 C 516 GLY GLY ASN VAL GLY ASP ASP CYS ASN VAL PRO ILE PRO
SEQRES 9 C 516 SER TRP VAL TRP ASN GLN LYS SER ASP ASP SER LEU TYR
SEQRES 10 C 516 PHE LYS SER GLU THR GLY THR VAL ASN LYS GLU THR LEU
SEQRES 11 C 516 ASN PRO LEU ALA SER ASP VAL ILE ARG LYS GLU TYR GLY
SEQRES 12 C 516 GLU LEU TYR THR ALA PHE ALA ALA ALA MET LYS PRO TYR
SEQRES 13 C 516 LYS ASP VAL ILE ALA LYS ILE TYR LEU SER GLY GLY PRO
SEQRES 14 C 516 ALA GLY GLU LEU ARG TYR PRO SER TYR THR THR SER ASP
SEQRES 15 C 516 GLY THR GLY TYR PRO SER ARG GLY LYS PHE GLN ALA TYR
SEQRES 16 C 516 THR GLU PHE ALA LYS SER LYS PHE ARG LEU TRP VAL LEU
SEQRES 17 C 516 ASN LYS TYR GLY SER LEU ASN GLU VAL ASN LYS ALA TRP
SEQRES 18 C 516 GLY THR LYS LEU ILE SER GLU LEU ALA ILE LEU PRO PRO
SEQRES 19 C 516 SER ASP GLY GLU GLN PHE LEU MET ASN GLY TYR LEU SER
SEQRES 20 C 516 MET TYR GLY LYS ASP TYR LEU GLU TRP TYR GLN GLY ILE
SEQRES 21 C 516 LEU GLU ASN HIS THR LYS LEU ILE GLY GLU LEU ALA HIS
SEQRES 22 C 516 ASN ALA PHE ASP THR THR PHE GLN VAL PRO ILE GLY ALA
SEQRES 23 C 516 LYS ILE ALA GLY VAL HIS TRP GLN TYR ASN ASN PRO THR
SEQRES 24 C 516 ILE PRO HIS GLY ALA GLU LYS PRO ALA GLY TYR ASN ASP
SEQRES 25 C 516 TYR SER HIS LEU LEU ASP ALA PHE LYS SER ALA LYS LEU
SEQRES 26 C 516 ASP VAL THR PHE THR CYS LEU GLU MET THR ASP LYS GLY
SEQRES 27 C 516 SER TYR PRO GLU TYR SER MET PRO LYS THR LEU VAL GLN
SEQRES 28 C 516 ASN ILE ALA THR LEU ALA ASN GLU LYS GLY ILE VAL LEU
SEQRES 29 C 516 ASN GLY GLU ASN ALA LEU SER ILE GLY ASN GLU GLU GLU
SEQRES 30 C 516 TYR LYS ARG VAL ALA GLU MET ALA PHE ASN TYR ASN PHE
SEQRES 31 C 516 ALA GLY PHE THR LEU LEU ARG TYR GLN ASP VAL MET TYR
SEQRES 32 C 516 ASN ASN SER LEU MET GLY LYS PHE LYS ASP LEU LEU GLY
SEQRES 33 C 516 VAL THR PRO VAL MET GLN THR ILE VAL VAL LYS ASN VAL
SEQRES 34 C 516 PRO THR THR ILE GLY ASP THR VAL TYR ILE THR GLY ASN
SEQRES 35 C 516 ARG ALA GLU LEU GLY SER TRP ASP THR LYS GLN TYR PRO
SEQRES 36 C 516 ILE GLN LEU TYR TYR ASP SER HIS SER ASN ASP TRP ARG
SEQRES 37 C 516 GLY ASN VAL VAL LEU PRO ALA GLU ARG ASN ILE GLU PHE
SEQRES 38 C 516 LYS ALA PHE ILE LYS SER LYS ASP GLY THR VAL LYS SER
SEQRES 39 C 516 TRP GLN THR ILE GLN GLN SER TRP ASN PRO VAL PRO LEU
SEQRES 40 C 516 LYS THR THR SER HIS THR SER SER TRP
SEQRES 1 D 516 ALA VAL ASN GLY LYS GLY MET ASN PRO ASP TYR LYS ALA
SEQRES 2 D 516 TYR LEU MET ALA PRO LEU LYS LYS ILE PRO GLU VAL THR
SEQRES 3 D 516 ASN TRP GLU THR PHE GLU ASN ASP LEU ARG TRP ALA LYS
SEQRES 4 D 516 GLN ASN GLY PHE TYR ALA ILE THR VAL ASP PHE TRP TRP
SEQRES 5 D 516 GLY ASP MET GLU LYS ASN GLY ASP GLN GLN PHE ASP PHE
SEQRES 6 D 516 SER TYR ALA GLN ARG PHE ALA GLN SER VAL LYS ASN ALA
SEQRES 7 D 516 GLY MET LYS MET ILE PRO ILE ILE SER THR HIS GLN CYS
SEQRES 8 D 516 GLY GLY ASN VAL GLY ASP ASP CYS ASN VAL PRO ILE PRO
SEQRES 9 D 516 SER TRP VAL TRP ASN GLN LYS SER ASP ASP SER LEU TYR
SEQRES 10 D 516 PHE LYS SER GLU THR GLY THR VAL ASN LYS GLU THR LEU
SEQRES 11 D 516 ASN PRO LEU ALA SER ASP VAL ILE ARG LYS GLU TYR GLY
SEQRES 12 D 516 GLU LEU TYR THR ALA PHE ALA ALA ALA MET LYS PRO TYR
SEQRES 13 D 516 LYS ASP VAL ILE ALA LYS ILE TYR LEU SER GLY GLY PRO
SEQRES 14 D 516 ALA GLY GLU LEU ARG TYR PRO SER TYR THR THR SER ASP
SEQRES 15 D 516 GLY THR GLY TYR PRO SER ARG GLY LYS PHE GLN ALA TYR
SEQRES 16 D 516 THR GLU PHE ALA LYS SER LYS PHE ARG LEU TRP VAL LEU
SEQRES 17 D 516 ASN LYS TYR GLY SER LEU ASN GLU VAL ASN LYS ALA TRP
SEQRES 18 D 516 GLY THR LYS LEU ILE SER GLU LEU ALA ILE LEU PRO PRO
SEQRES 19 D 516 SER ASP GLY GLU GLN PHE LEU MET ASN GLY TYR LEU SER
SEQRES 20 D 516 MET TYR GLY LYS ASP TYR LEU GLU TRP TYR GLN GLY ILE
SEQRES 21 D 516 LEU GLU ASN HIS THR LYS LEU ILE GLY GLU LEU ALA HIS
SEQRES 22 D 516 ASN ALA PHE ASP THR THR PHE GLN VAL PRO ILE GLY ALA
SEQRES 23 D 516 LYS ILE ALA GLY VAL HIS TRP GLN TYR ASN ASN PRO THR
SEQRES 24 D 516 ILE PRO HIS GLY ALA GLU LYS PRO ALA GLY TYR ASN ASP
SEQRES 25 D 516 TYR SER HIS LEU LEU ASP ALA PHE LYS SER ALA LYS LEU
SEQRES 26 D 516 ASP VAL THR PHE THR CYS LEU GLU MET THR ASP LYS GLY
SEQRES 27 D 516 SER TYR PRO GLU TYR SER MET PRO LYS THR LEU VAL GLN
SEQRES 28 D 516 ASN ILE ALA THR LEU ALA ASN GLU LYS GLY ILE VAL LEU
SEQRES 29 D 516 ASN GLY GLU ASN ALA LEU SER ILE GLY ASN GLU GLU GLU
SEQRES 30 D 516 TYR LYS ARG VAL ALA GLU MET ALA PHE ASN TYR ASN PHE
SEQRES 31 D 516 ALA GLY PHE THR LEU LEU ARG TYR GLN ASP VAL MET TYR
SEQRES 32 D 516 ASN ASN SER LEU MET GLY LYS PHE LYS ASP LEU LEU GLY
SEQRES 33 D 516 VAL THR PRO VAL MET GLN THR ILE VAL VAL LYS ASN VAL
SEQRES 34 D 516 PRO THR THR ILE GLY ASP THR VAL TYR ILE THR GLY ASN
SEQRES 35 D 516 ARG ALA GLU LEU GLY SER TRP ASP THR LYS GLN TYR PRO
SEQRES 36 D 516 ILE GLN LEU TYR TYR ASP SER HIS SER ASN ASP TRP ARG
SEQRES 37 D 516 GLY ASN VAL VAL LEU PRO ALA GLU ARG ASN ILE GLU PHE
SEQRES 38 D 516 LYS ALA PHE ILE LYS SER LYS ASP GLY THR VAL LYS SER
SEQRES 39 D 516 TRP GLN THR ILE GLN GLN SER TRP ASN PRO VAL PRO LEU
SEQRES 40 D 516 LYS THR THR SER HIS THR SER SER TRP
HET CA A 601 1
HET CA B 602 1
HET CA C 603 1
HET CA D 604 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 4(CA 2+)
FORMUL 9 HOH *752(H2 O)
HELIX 1 1 VAL A 2 GLY A 4 5 3
HELIX 2 2 ILE A 22 VAL A 25 1 4
HELIX 3 3 TRP A 28 GLN A 40 1 13
HELIX 4 4 TRP A 52 MET A 55 1 4
HELIX 5 5 SER A 66 ASN A 77 1 12
HELIX 6 6 SER A 105 GLN A 110 5 6
HELIX 7 7 SER A 135 VAL A 159 1 25
HELIX 8 8 PRO A 169 GLY A 171 5 3
HELIX 9 9 GLU A 197 TYR A 211 1 15
HELIX 10 10 LEU A 214 TRP A 221 1 8
HELIX 11 11 GLU A 228 ALA A 230 5 3
HELIX 12 12 GLY A 237 MET A 242 1 6
HELIX 13 13 GLY A 244 LEU A 246 5 3
HELIX 14 14 MET A 248 PHE A 280 1 33
HELIX 15 15 GLU A 305 ALA A 308 1 4
HELIX 16 16 TYR A 313 ALA A 323 1 11
HELIX 17 17 PRO A 346 LYS A 360 1 15
HELIX 18 18 GLU A 375 ASN A 387 1 13
HELIX 19 19 TYR A 398 MET A 402 1 5
HELIX 20 20 ASN A 405 LEU A 414 1 10
HELIX 21 21 ALA A 444 LEU A 446 5 3
HELIX 22 22 VAL B 2 GLY B 4 5 3
HELIX 23 23 ILE B 22 VAL B 25 1 4
HELIX 24 24 TRP B 28 ASN B 41 1 14
HELIX 25 25 TRP B 52 MET B 55 1 4
HELIX 26 26 SER B 66 ALA B 78 1 13
HELIX 27 27 SER B 105 GLN B 110 5 6
HELIX 28 28 SER B 135 VAL B 159 1 25
HELIX 29 29 PRO B 169 GLY B 171 5 3
HELIX 30 30 GLU B 197 TYR B 211 1 15
HELIX 31 31 LEU B 214 ALA B 220 1 7
HELIX 32 32 GLU B 228 ALA B 230 5 3
HELIX 33 33 GLY B 237 MET B 242 1 6
HELIX 34 34 GLY B 244 LEU B 246 5 3
HELIX 35 35 MET B 248 PHE B 280 1 33
HELIX 36 36 GLU B 305 ALA B 308 1 4
HELIX 37 37 TYR B 313 SER B 322 1 10
HELIX 38 38 PRO B 346 LYS B 360 1 15
HELIX 39 39 GLU B 375 ASN B 387 1 13
HELIX 40 40 TYR B 398 MET B 402 1 5
HELIX 41 41 ASN B 405 LEU B 415 1 11
HELIX 42 42 ALA B 444 LEU B 446 5 3
HELIX 43 43 VAL C 2 GLY C 4 5 3
HELIX 44 44 ILE C 22 VAL C 25 1 4
HELIX 45 45 TRP C 28 GLN C 40 1 13
HELIX 46 46 TRP C 52 MET C 55 1 4
HELIX 47 47 SER C 66 ASN C 77 1 12
HELIX 48 48 SER C 105 GLN C 110 5 6
HELIX 49 49 SER C 135 ALA C 152 1 18
HELIX 50 50 LYS C 154 VAL C 159 5 6
HELIX 51 51 PRO C 169 GLY C 171 5 3
HELIX 52 52 GLU C 197 TYR C 211 1 15
HELIX 53 53 LEU C 214 TRP C 221 1 8
HELIX 54 54 GLU C 228 ALA C 230 5 3
HELIX 55 55 GLY C 237 MET C 242 1 6
HELIX 56 56 GLY C 244 LEU C 246 5 3
HELIX 57 57 MET C 248 PHE C 280 1 33
HELIX 58 58 GLU C 305 ALA C 308 1 4
HELIX 59 59 TYR C 313 ALA C 323 1 11
HELIX 60 60 PRO C 346 LYS C 360 1 15
HELIX 61 61 GLU C 375 ASN C 387 1 13
HELIX 62 62 TYR C 398 MET C 402 1 5
HELIX 63 63 ASN C 405 LEU C 414 1 10
HELIX 64 64 ALA C 444 LEU C 446 5 3
HELIX 65 65 VAL D 2 GLY D 4 5 3
HELIX 66 66 ILE D 22 VAL D 25 1 4
HELIX 67 67 TRP D 28 ASN D 41 1 14
HELIX 68 68 TRP D 52 MET D 55 1 4
HELIX 69 69 SER D 66 ALA D 78 1 13
HELIX 70 70 SER D 105 GLN D 110 5 6
HELIX 71 71 SER D 135 VAL D 159 1 25
HELIX 72 72 PRO D 169 GLY D 171 5 3
HELIX 73 73 GLU D 197 TYR D 211 1 15
HELIX 74 74 LEU D 214 ALA D 220 1 7
HELIX 75 75 GLU D 228 ALA D 230 5 3
HELIX 76 76 GLY D 237 MET D 242 1 6
HELIX 77 77 GLY D 244 LEU D 246 5 3
HELIX 78 78 MET D 248 PHE D 276 1 29
HELIX 79 79 GLU D 305 ALA D 308 1 4
HELIX 80 80 TYR D 313 ALA D 323 1 11
HELIX 81 81 PRO D 346 LYS D 360 1 15
HELIX 82 82 GLU D 375 ASN D 387 1 13
HELIX 83 83 TYR D 398 MET D 402 1 5
HELIX 84 84 ASN D 405 LEU D 414 1 10
HELIX 85 85 ALA D 444 LEU D 446 5 3
SHEET 1 A 9 LYS A 12 LEU A 15 0
SHEET 2 A 9 GLY A 392 LEU A 395 1 N PHE A 393 O LYS A 12
SHEET 3 A 9 LEU A 364 GLU A 367 1 N GLY A 366 O GLY A 392
SHEET 4 A 9 ASP A 326 PHE A 329 1 N VAL A 327 O ASN A 365
SHEET 5 A 9 PRO A 283 LYS A 287 1 N ALA A 286 O ASP A 326
SHEET 6 A 9 ILE A 160 LEU A 165 1 N ILE A 163 O PRO A 283
SHEET 7 A 9 LYS A 81 SER A 87 1 N MET A 82 O ALA A 161
SHEET 8 A 9 PHE A 43 TRP A 51 1 N ILE A 46 O LYS A 81
SHEET 9 A 9 ALA A 13 MET A 16 1 N ALA A 13 O TYR A 44
SHEET 1 B 4 SER A 511 SER A 515 0
SHEET 2 B 4 PRO A 419 LYS A 427 1 N THR A 423 O HIS A 512
SHEET 3 B 4 ASP A 466 PRO A 474 -1 N LEU A 473 O VAL A 420
SHEET 4 B 4 TYR A 459 ASP A 461 -1 N ASP A 461 O ASP A 466
SHEET 1 C 3 THR A 436 GLY A 441 0
SHEET 2 C 3 ILE A 479 LYS A 486 -1 N LYS A 486 O THR A 436
SHEET 3 C 3 GLN A 500 TRP A 502 -1 N TRP A 502 O ILE A 479
SHEET 1 D 2 PHE A 484 LYS A 486 0
SHEET 2 D 2 VAL A 492 TRP A 495 -1 N SER A 494 O ILE A 485
SHEET 1 E 8 ILE B 160 LEU B 165 0
SHEET 2 E 8 LYS B 81 SER B 87 1 N MET B 82 O ALA B 161
SHEET 3 E 8 ALA B 45 TRP B 51 1 N ILE B 46 O LYS B 81
SHEET 4 E 8 LYS B 12 MET B 16 1 N LEU B 15 O ALA B 45
SHEET 5 E 8 GLY B 392 LEU B 395 1 N PHE B 393 O LYS B 12
SHEET 6 E 8 LEU B 364 GLU B 367 1 N GLY B 366 O GLY B 392
SHEET 7 E 8 ASP B 326 THR B 330 1 N VAL B 327 O ASN B 365
SHEET 8 E 8 GLY B 285 LYS B 287 1 N ALA B 286 O ASP B 326
SHEET 1 F 4 SER B 511 SER B 515 0
SHEET 2 F 4 PRO B 419 LYS B 427 1 N THR B 423 O HIS B 512
SHEET 3 F 4 ASP B 466 PRO B 474 -1 N LEU B 473 O VAL B 420
SHEET 4 F 4 TYR B 459 ASP B 461 -1 N ASP B 461 O ASP B 466
SHEET 1 G 3 THR B 436 GLY B 441 0
SHEET 2 G 3 ILE B 479 LYS B 486 -1 N LYS B 486 O THR B 436
SHEET 3 G 3 GLN B 500 TRP B 502 -1 N TRP B 502 O ILE B 479
SHEET 1 H 2 PHE B 484 LYS B 486 0
SHEET 2 H 2 VAL B 492 TRP B 495 -1 N SER B 494 O ILE B 485
SHEET 1 I 9 LYS C 12 LEU C 15 0
SHEET 2 I 9 GLY C 392 LEU C 395 1 N PHE C 393 O LYS C 12
SHEET 3 I 9 LEU C 364 GLU C 367 1 N GLY C 366 O GLY C 392
SHEET 4 I 9 ASP C 326 PHE C 329 1 N VAL C 327 O ASN C 365
SHEET 5 I 9 PRO C 283 LYS C 287 1 N ALA C 286 O ASP C 326
SHEET 6 I 9 ILE C 160 LEU C 165 1 N ILE C 163 O PRO C 283
SHEET 7 I 9 LYS C 81 SER C 87 1 N MET C 82 O ALA C 161
SHEET 8 I 9 PHE C 43 TRP C 51 1 N ILE C 46 O LYS C 81
SHEET 9 I 9 ALA C 13 MET C 16 1 N ALA C 13 O TYR C 44
SHEET 1 J 4 SER C 511 SER C 515 0
SHEET 2 J 4 PRO C 419 LYS C 427 1 N THR C 423 O HIS C 512
SHEET 3 J 4 ASP C 466 PRO C 474 -1 N LEU C 473 O VAL C 420
SHEET 4 J 4 TYR C 459 ASP C 461 -1 N ASP C 461 O ASP C 466
SHEET 1 K 3 THR C 436 GLY C 441 0
SHEET 2 K 3 ILE C 479 LYS C 486 -1 N LYS C 486 O THR C 436
SHEET 3 K 3 GLN C 500 TRP C 502 -1 N TRP C 502 O ILE C 479
SHEET 1 L 2 PHE C 484 LYS C 486 0
SHEET 2 L 2 VAL C 492 TRP C 495 -1 N SER C 494 O ILE C 485
SHEET 1 M 9 LYS D 12 LEU D 15 0
SHEET 2 M 9 GLY D 392 LEU D 395 1 N PHE D 393 O LYS D 12
SHEET 3 M 9 LEU D 364 GLU D 367 1 N GLY D 366 O GLY D 392
SHEET 4 M 9 ASP D 326 PHE D 329 1 N VAL D 327 O ASN D 365
SHEET 5 M 9 PRO D 283 ILE D 288 1 N ALA D 286 O ASP D 326
SHEET 6 M 9 ILE D 160 LEU D 165 1 N ILE D 163 O PRO D 283
SHEET 7 M 9 LYS D 81 SER D 87 1 N MET D 82 O ALA D 161
SHEET 8 M 9 PHE D 43 TRP D 51 1 N ILE D 46 O LYS D 81
SHEET 9 M 9 ALA D 13 MET D 16 1 N ALA D 13 O TYR D 44
SHEET 1 N 4 SER D 511 SER D 515 0
SHEET 2 N 4 PRO D 419 LYS D 427 1 N THR D 423 O HIS D 512
SHEET 3 N 4 ASP D 466 PRO D 474 -1 N LEU D 473 O VAL D 420
SHEET 4 N 4 TYR D 459 ASP D 461 -1 N ASP D 461 O ASP D 466
SHEET 1 O 3 THR D 436 GLY D 441 0
SHEET 2 O 3 ILE D 479 LYS D 486 -1 N LYS D 486 O THR D 436
SHEET 3 O 3 GLN D 500 TRP D 502 -1 N TRP D 502 O ILE D 479
SHEET 1 P 2 PHE D 484 LYS D 486 0
SHEET 2 P 2 VAL D 492 TRP D 495 -1 N SER D 494 O ILE D 485
SSBOND 1 CYS A 91 CYS A 99 1555 1555 2.04
SSBOND 2 CYS B 91 CYS B 99 1555 1555 2.08
SSBOND 3 CYS C 91 CYS C 99 1555 1555 2.04
SSBOND 4 CYS D 91 CYS D 99 1555 1555 2.02
LINK OE2 GLU A 56 CA CA A 601 1555 1555 2.33
LINK OD1 ASP A 60 CA CA A 601 1555 1555 2.42
LINK OE1 GLN A 61 CA CA A 601 1555 1555 2.62
LINK OE1 GLU A 141 CA CA A 601 1555 1555 2.31
LINK OE1 GLU A 144 CA CA A 601 1555 1555 2.15
LINK CA CA A 601 O HOH A 602 1555 1555 2.50
LINK OE2 GLU B 56 CA CA B 602 1555 1555 2.39
LINK OD1 ASP B 60 CA CA B 602 1555 1555 2.30
LINK OE1 GLN B 61 CA CA B 602 1555 1555 2.46
LINK OE1 GLU B 141 CA CA B 602 1555 1555 2.41
LINK OE1 GLU B 144 CA CA B 602 1555 1555 2.44
LINK CA CA B 602 O HOH B 603 1555 1555 2.47
LINK OE2 GLU C 56 CA CA C 603 1555 1555 2.20
LINK OD1 ASP C 60 CA CA C 603 1555 1555 2.39
LINK OE1 GLN C 61 CA CA C 603 1555 1555 2.55
LINK OE1 GLU C 141 CA CA C 603 1555 1555 2.48
LINK OE1 GLU C 144 CA CA C 603 1555 1555 2.20
LINK CA CA C 603 O HOH C 604 1555 1555 2.42
LINK OE2 GLU D 56 CA CA D 604 1555 1555 2.36
LINK OD1 ASP D 60 CA CA D 604 1555 1555 2.06
LINK OE1 GLN D 61 CA CA D 604 1555 1555 2.19
LINK OE1 GLU D 141 CA CA D 604 1555 1555 2.49
LINK OE1 GLU D 144 CA CA D 604 1555 1555 2.24
LINK CA CA D 604 O HOH D 605 1555 1555 1.93
CISPEP 1 TYR A 186 PRO A 187 0 -0.15
CISPEP 2 TYR A 340 PRO A 341 0 0.55
CISPEP 3 LEU A 396 ARG A 397 0 9.64
CISPEP 4 ASN A 503 PRO A 504 0 -1.28
CISPEP 5 TYR B 186 PRO B 187 0 -4.52
CISPEP 6 TYR B 340 PRO B 341 0 0.31
CISPEP 7 LEU B 396 ARG B 397 0 6.77
CISPEP 8 ASN B 503 PRO B 504 0 -2.05
CISPEP 9 TYR C 186 PRO C 187 0 2.00
CISPEP 10 TYR C 340 PRO C 341 0 -4.24
CISPEP 11 LEU C 396 ARG C 397 0 7.38
CISPEP 12 ASN C 503 PRO C 504 0 -6.31
CISPEP 13 TYR D 186 PRO D 187 0 -3.38
CISPEP 14 TYR D 340 PRO D 341 0 -1.73
CISPEP 15 LEU D 396 ARG D 397 0 18.01
CISPEP 16 ASN D 503 PRO D 504 0 -0.31
SITE 1 CAA 2 GLU A 172 GLU A 367
SITE 1 CAB 2 GLU B 172 GLU B 367
SITE 1 CAC 2 GLU C 172 GLU C 367
SITE 1 CAD 2 GLU D 172 GLU D 367
SITE 1 AC1 6 GLU A 56 ASP A 60 GLN A 61 GLU A 141
SITE 2 AC1 6 GLU A 144 HOH A 602
SITE 1 AC2 6 GLU B 56 ASP B 60 GLN B 61 GLU B 141
SITE 2 AC2 6 GLU B 144 HOH B 603
SITE 1 AC3 6 GLU C 56 ASP C 60 GLN C 61 GLU C 141
SITE 2 AC3 6 GLU C 144 HOH C 604
SITE 1 AC4 6 GLU D 56 ASP D 60 GLN D 61 GLU D 141
SITE 2 AC4 6 GLU D 144 HOH D 605
CRYST1 177.900 112.900 146.200 90.00 105.80 90.00 C 1 2 1 16
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 0.005621 0.000000 0.001591 0.00000
SCALE2 0.000000 0.008857 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007108 0.00000
MTRIX1 1 0.705536 -0.458632 0.540255 9.39680 1
MTRIX2 1 -0.462537 0.279566 0.841369 42.06810 1
MTRIX3 1 -0.536916 -0.843504 -0.014890 68.03210 1
MTRIX1 2 -0.950033 0.071478 0.303856 71.95160 1
MTRIX2 2 0.085982 -0.875849 0.474864 60.86340 1
MTRIX3 2 0.300075 0.477262 0.825939 -28.05910 1
MTRIX1 3 -0.869138 0.207822 -0.448787 86.66920 1
MTRIX2 3 0.206265 -0.672425 -0.710844 57.92760 1
MTRIX3 3 -0.449505 -0.710391 0.541563 51.88800 1
(ATOM LINES ARE NOT SHOWN.)
END
