HEADER LYASE(CARBON-CARBON) 28-NOV-90 9RUB
TITLE CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE
TITLE 2 CARBOXYLASE COMPLEXED WITH ITS SUBSTRATE, RIBULOSE-1,5-
TITLE 3 BISPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 4.1.1.39;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;
SOURCE 3 ORGANISM_TAXID: 1085
KEYWDS LYASE(CARBON-CARBON)
EXPDTA X-RAY DIFFRACTION
AUTHOR T.LUNDQVIST,G.SCHNEIDER
REVDAT 3 24-FEB-09 9RUB 1 VERSN
REVDAT 2 15-JAN-95 9RUB 1 COMPND
REVDAT 1 15-JAN-93 9RUB 0
JRNL AUTH T.LUNDQVIST,G.SCHNEIDER
JRNL TITL CRYSTAL STRUCTURE OF ACTIVATED
JRNL TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE COMPLEXED
JRNL TITL 3 WITH ITS SUBSTRATE, RIBULOSE-1,5-BISPHOSPHATE.
JRNL REF J.BIOL.CHEM. V. 266 12604 1991
JRNL REFN ISSN 0021-9258
JRNL PMID 1905726
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.SCHNEIDER,S.KNIGHT,I.ANDERSSON,Y.LINDQVIST,
REMARK 1 AUTH 2 T.LUNDQVIST,C.-I.BRANDEN
REMARK 1 TITL COMPARISON OF THE CRYSTAL STRUCTURES OF L2 AND
REMARK 1 TITL 2 L8S8 RUBISCO SUGGESTS A FUNCTIONAL ROLE FOR THE
REMARK 1 TITL 3 SMALL SUBUNIT
REMARK 1 REF EMBO J. V. 9 2045 1990
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.SCHNEIDER,Y.LINDQVIST,T.LUNDQVIST
REMARK 1 TITL CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE FROM
REMARK 1 TITL 3 RHODOSPIRILLUM RUBRUM AT 1.7 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 211 989 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.LUNDQVIST,G.SCHNEIDER
REMARK 1 TITL CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND A
REMARK 1 TITL 3 TRANSITION STATE ANALOGUE, 2-CARBOXY-D-ARABINITOL
REMARK 1 TITL 4 1,5-BISPHOSPHATE
REMARK 1 REF J.BIOL.CHEM. V. 264 7078 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH T.LUNDQVIST,G.SCHNEIDER
REMARK 1 TITL CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS
REMARK 1 TITL 3 PRODUCT, 3-PHOSPHO-D-GLYCERATE
REMARK 1 REF J.BIOL.CHEM. V. 264 3643 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.SCHNEIDER,Y.LINDQVIST,C.-I.BRANDEN,G.LORIMER
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)
REMARK 1 TITL 3 OXYGENASE FROM RHODOSPIRILLUM RUBRUM AT 2.9
REMARK 1 TITL 4 ANGSTROMS RESOLUTION
REMARK 1 REF EMBO J. V. 5 3409 1986
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 0
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.017 ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; 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: RESIDUES A 191 AND B 191 ARE
REMARK 3 MODIFIED LYSINES WHICH ARE CARBAMYLATED AT THE EPSILON-AMINO
REMARK 3 GROUP. THE CARBAMYL GROUPS ARE PRESENTED AS HET GROUPS *CBX*
REMARK 3 AT THE END OF CHAINS *A* AND *B*.
REMARK 4
REMARK 4 9RUB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 35.30000
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 300 REMARK:
REMARK 300 THE TRANSFORMATION GIVEN ON THE *MTRIX* RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO
REMARK 300 COORDINATES OF CHAIN *B*. RESIDUES 422 - 450 WERE OMITTED
REMARK 300 WHEN GENERATING THIS TRANSFORMATION MATRIX.
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: 8750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 MET A 1
REMARK 465 ARG A 461
REMARK 465 SER A 462
REMARK 465 ALA A 463
REMARK 465 LEU A 464
REMARK 465 PRO A 465
REMARK 465 ALA A 466
REMARK 465 MET B 1
REMARK 465 THR B 460
REMARK 465 ARG B 461
REMARK 465 SER B 462
REMARK 465 ALA B 463
REMARK 465 LEU B 464
REMARK 465 PRO B 465
REMARK 465 ALA B 466
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 460 CB OG1 CG2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 458 CD OE1 OE2
REMARK 480 ASP A 459 CG OD1
REMARK 480 THR A 460 CA C O
REMARK 480 VAL B 457 O
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 O SER A 356 N GLY A 358 2.12
REMARK 500 OH TYR B 7 OG1 THR B 51 2.12
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 458 CG GLU A 458 CD 0.324
REMARK 500 ASP A 459 CG ASP A 459 OD2 0.311
REMARK 500 THR A 460 N THR A 460 CA -0.205
REMARK 500 VAL B 457 C VAL B 457 O -0.175
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 SER A 4 N - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 SER A 4 C - N - CA ANGL. DEV. = 21.0 DEGREES
REMARK 500 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 6 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 LEU A 10 N - CA - C ANGL. DEV. = -18.5 DEGREES
REMARK 500 GLU A 22 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 GLU A 22 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 LEU A 25 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 TYR A 38 C - N - CA ANGL. DEV. = 17.2 DEGREES
REMARK 500 ASN A 54 CA - CB - CG ANGL. DEV. = 20.6 DEGREES
REMARK 500 VAL A 55 CA - CB - CG2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU A 56 CA - C - O ANGL. DEV. = 18.2 DEGREES
REMARK 500 GLU A 56 O - C - N ANGL. DEV. = -12.9 DEGREES
REMARK 500 VAL A 57 C - N - CA ANGL. DEV. = 36.0 DEGREES
REMARK 500 CYS A 58 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 CYS A 58 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 THR A 59 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 THR A 59 C - N - CA ANGL. DEV. = 19.9 DEGREES
REMARK 500 THR A 60 C - N - CA ANGL. DEV. = 18.3 DEGREES
REMARK 500 ASP A 61 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 62 CB - CG - OD2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 ASP A 62 C - N - CA ANGL. DEV. = 18.2 DEGREES
REMARK 500 THR A 64 N - CA - CB ANGL. DEV. = 12.3 DEGREES
REMARK 500 THR A 64 CA - C - O ANGL. DEV. = 17.5 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 THR A 64 CA - C - N ANGL. DEV. = -13.8 DEGREES
REMARK 500 ARG A 65 C - N - CA ANGL. DEV. = 22.1 DEGREES
REMARK 500 VAL A 67 C - N - CA ANGL. DEV. = 21.6 DEGREES
REMARK 500 ASP A 68 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 VAL A 71 N - CA - CB ANGL. DEV. = 20.6 DEGREES
REMARK 500 TYR A 72 CB - CG - CD2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 75 N - CA - CB ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP A 75 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 ARG A 78 CD - NE - CZ ANGL. DEV. = 32.4 DEGREES
REMARK 500 ARG A 78 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 PHE A 90 CB - CG - CD2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 91 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 THR A 95 CA - CB - CG2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASP A 96 CB - CG - OD1 ANGL. DEV. = 18.7 DEGREES
REMARK 500 ASP A 96 CB - CG - OD2 ANGL. DEV. = -12.0 DEGREES
REMARK 500 LYS A 98 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 PHE A 104 CB - CG - CD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 LEU A 105 CA - C - O ANGL. DEV. = -15.6 DEGREES
REMARK 500 THR A 106 N - CA - CB ANGL. DEV. = 21.2 DEGREES
REMARK 500 LEU A 105 CA - C - N ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASN A 112 CA - CB - CG ANGL. DEV. = 13.3 DEGREES
REMARK 500 MET A 115 CB - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 MET A 115 CA - CB - CG ANGL. DEV. = 10.5 DEGREES
REMARK 500 ASP A 117 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 398 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 GLN A 3 -155.03 65.79
REMARK 500 SER A 4 -91.70 -149.47
REMARK 500 SER A 5 145.60 -29.90
REMARK 500 ARG A 6 -35.05 79.52
REMARK 500 ASN A 9 61.69 -171.07
REMARK 500 ALA A 11 -8.52 146.95
REMARK 500 TYR A 38 -80.36 21.15
REMARK 500 SER A 50 -97.10 -139.34
REMARK 500 THR A 53 67.31 31.27
REMARK 500 VAL A 55 -119.67 61.27
REMARK 500 ASP A 62 132.14 80.95
REMARK 500 PHE A 63 91.47 78.02
REMARK 500 THR A 64 77.56 -151.31
REMARK 500 VAL A 67 20.12 -151.24
REMARK 500 PRO A 86 159.09 -49.85
REMARK 500 ASP A 96 -16.59 -140.77
REMARK 500 MET A 115 135.99 -37.56
REMARK 500 PRO A 129 169.77 -25.81
REMARK 500 PHE A 136 139.73 156.16
REMARK 500 ASP A 137 -70.86 -50.38
REMARK 500 SER A 144 15.55 -52.39
REMARK 500 LYS A 148 -7.32 -59.15
REMARK 500 ASP A 156 19.41 24.52
REMARK 500 LEU A 169 143.85 -170.75
REMARK 500 LEU A 171 100.04 8.50
REMARK 500 ARG A 172 -179.07 -54.05
REMARK 500 TRP A 184 16.40 -65.05
REMARK 500 PRO A 195 42.33 -84.01
REMARK 500 ALA A 202 75.91 -151.52
REMARK 500 LEU A 204 -60.53 -13.99
REMARK 500 ASP A 220 -77.71 -106.74
REMARK 500 GLU A 221 -2.55 -51.15
REMARK 500 ASP A 263 14.86 -67.10
REMARK 500 TYR A 265 -63.17 -97.65
REMARK 500 VAL A 266 40.11 -60.43
REMARK 500 ALA A 267 4.58 176.80
REMARK 500 ARG A 288 40.43 -57.43
REMARK 500 ALA A 289 151.06 -44.70
REMARK 500 VAL A 294 -72.29 -105.67
REMARK 500 PRO A 297 8.55 -58.32
REMARK 500 HIS A 321 78.92 -69.72
REMARK 500 THR A 324 148.16 176.41
REMARK 500 PHE A 327 -143.85 -130.60
REMARK 500 LYS A 329 -108.01 62.56
REMARK 500 GLU A 333 54.66 2.21
REMARK 500 SER A 334 72.69 75.12
REMARK 500 ALA A 338 -56.20 -28.63
REMARK 500 GLU A 347 60.70 -174.20
REMARK 500 PRO A 351 2.20 -56.60
REMARK 500 PHE A 352 -48.37 -157.36
REMARK 500 SER A 356 47.49 -102.74
REMARK 500 TRP A 357 12.37 -19.45
REMARK 500 MET A 360 -123.97 -60.26
REMARK 500 LYS A 361 -156.87 -164.38
REMARK 500 ASN A 372 -177.56 -49.59
REMARK 500 ALA A 373 -62.01 -18.64
REMARK 500 PHE A 380 -17.74 -48.35
REMARK 500 LEU A 383 -89.68 -83.65
REMARK 500 ASN A 385 -168.92 -170.92
REMARK 500 ALA A 386 19.10 -149.75
REMARK 500 PRO A 403 11.93 -56.21
REMARK 500 ARG A 418 -76.83 -44.45
REMARK 500 PRO A 422 125.89 40.46
REMARK 500 PHE A 440 66.60 -118.65
REMARK 500 ASP A 443 -57.44 -123.57
REMARK 500 ALA A 444 74.19 -65.90
REMARK 500 ASP A 445 -84.89 171.48
REMARK 500 PRO A 449 -80.38 16.51
REMARK 500 TRP A 451 -33.92 -17.87
REMARK 500 ARG A 452 -70.44 -48.73
REMARK 500 VAL A 457 -157.64 118.72
REMARK 500 ASP A 459 155.46 127.79
REMARK 500 GLN B 3 -25.44 53.19
REMARK 500 SER B 4 170.94 131.96
REMARK 500 SER B 5 17.17 -155.76
REMARK 500 ASN B 9 83.68 -168.05
REMARK 500 SER B 50 -89.98 -108.21
REMARK 500 THR B 53 72.51 63.12
REMARK 500 ASN B 54 -87.80 -17.64
REMARK 500 GLU B 56 -103.39 87.92
REMARK 500 CYS B 58 -34.01 -28.13
REMARK 500 THR B 59 -157.69 51.28
REMARK 500 ASP B 61 168.05 66.14
REMARK 500 ASP B 62 87.42 84.24
REMARK 500 PHE B 63 -22.69 110.00
REMARK 500 GLU B 73 141.88 -170.94
REMARK 500 GLU B 79 65.16 70.23
REMARK 500 PRO B 86 147.72 -37.49
REMARK 500 ASP B 91 110.93 71.83
REMARK 500 ALA B 99 176.81 -54.76
REMARK 500 LEU B 107 -73.22 -72.23
REMARK 500 MET B 109 59.81 -158.04
REMARK 500 ASN B 111 23.91 -74.94
REMARK 500 MET B 115 123.24 -170.59
REMARK 500 TYR B 120 131.24 65.43
REMARK 500 ASP B 125 138.70 150.32
REMARK 500 ASP B 137 -75.70 -66.70
REMARK 500 GLU B 154 0.37 -56.71
REMARK 500 LYS B 191 -88.71 -88.23
REMARK 500 ASN B 192 121.29 124.03
REMARK 500 GLU B 194 -56.77 -28.29
REMARK 500 ALA B 202 62.10 167.84
REMARK 500 ASP B 213 -70.84 -66.98
REMARK 500 ALA B 214 9.18 -52.84
REMARK 500 ASP B 235 -60.36 -103.38
REMARK 500 ARG B 243 -76.04 -86.98
REMARK 500 TYR B 246 -79.64 -63.16
REMARK 500 ALA B 267 -17.09 -140.92
REMARK 500 ALA B 269 -10.35 -39.29
REMARK 500 ARG B 276 -130.04 -72.30
REMARK 500 ARG B 277 -49.33 11.55
REMARK 500 PHE B 279 77.74 -115.67
REMARK 500 ARG B 288 -87.47 -73.53
REMARK 500 ALA B 289 -122.24 106.05
REMARK 500 THR B 322 -145.66 -153.73
REMARK 500 PHE B 327 175.86 143.99
REMARK 500 MET B 330 14.72 160.70
REMARK 500 GLU B 333 -168.81 -106.62
REMARK 500 SER B 335 18.85 7.93
REMARK 500 ALA B 338 2.00 -65.33
REMARK 500 PHE B 352 -33.18 -137.50
REMARK 500 ALA B 373 -4.29 -50.54
REMARK 500 ASN B 385 -169.56 -127.60
REMARK 500 PRO B 403 -84.64 -37.14
REMARK 500 PRO B 422 52.80 -63.94
REMARK 500 VAL B 423 -55.76 44.05
REMARK 500 ARG B 428 94.43 -68.75
REMARK 500 GLU B 429 -46.83 143.48
REMARK 500 LEU B 433 -70.24 -59.45
REMARK 500 PHE B 440 78.61 -112.57
REMARK 500 ALA B 444 -76.13 -68.31
REMARK 500 ASP B 445 26.39 -46.91
REMARK 500 GLN B 446 -18.87 -159.53
REMARK 500 GLU B 458 158.97 8.55
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, 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 VAL B 457 16.99
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 MG A 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 RUB A 600 O2
REMARK 620 2 RUB A 600 O3 73.1
REMARK 620 3 ASP A 193 OD1 102.9 154.1
REMARK 620 4 FMT A 601 O1 144.2 74.4 99.8
REMARK 620 5 FMT A 601 O2 124.5 105.9 54.5 52.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT B 701 O1
REMARK 620 2 ASP B 193 OD1 66.6
REMARK 620 3 RUB B 700 O3 74.4 137.9
REMARK 620 4 RUB B 700 O2 145.0 147.0 74.8
REMARK 620 N 1 2 3
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEETS *ACT* AND *BCT* PRESENTED BELOW ARE ACTUALLY
REMARK 700 EIGHT-STRANDED BETA/ALPHA BARRELS. THESE ARE REPRESENTED
REMARK 700 AS NINE-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CHAIN A
REMARK 800 SITE_IDENTIFIER: BCT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CHAIN B
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB A 600
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB B 700
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 601
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 701
DBREF 9RUB A 1 466 UNP P04718 RBL2_RHORU 1 466
DBREF 9RUB B 1 466 UNP P04718 RBL2_RHORU 1 466
SEQADV 9RUB ASP A 91 UNP P04718 HIS 91 CONFLICT
SEQADV 9RUB ASP B 91 UNP P04718 HIS 91 CONFLICT
SEQRES 1 A 466 MET ASP GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS
SEQRES 2 A 466 GLU GLU ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS
SEQRES 3 A 466 ALA TYR ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL
SEQRES 4 A 466 ALA THR ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY
SEQRES 5 A 466 THR ASN VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG
SEQRES 6 A 466 GLY VAL ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG
SEQRES 7 A 466 GLU LEU THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP
SEQRES 8 A 466 ARG ASN ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE
SEQRES 9 A 466 LEU THR LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP
SEQRES 10 A 466 VAL GLU TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU
SEQRES 11 A 466 ALA TYR ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE
SEQRES 12 A 466 SER ALA LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP
SEQRES 13 A 466 GLY GLY LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU
SEQRES 14 A 466 GLY LEU ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA
SEQRES 15 A 466 PHE TRP LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO
SEQRES 16 A 466 GLN GLY ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE
SEQRES 17 A 466 ALA LEU VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU
SEQRES 18 A 466 THR GLY GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA
SEQRES 19 A 466 ASP ASP PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL
SEQRES 20 A 466 LEU GLU THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU
SEQRES 21 A 466 LEU VAL ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR
SEQRES 22 A 466 THR ALA ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR
SEQRES 23 A 466 HIS ARG ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER
SEQRES 24 A 466 LYS ARG GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA
SEQRES 25 A 466 ARG LEU GLN GLY ALA SER GLY ILE HIS THR GLY THR MET
SEQRES 26 A 466 GLY PHE GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA
SEQRES 27 A 466 ILE ALA TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO
SEQRES 28 A 466 PHE TYR ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR
SEQRES 29 A 466 PRO ILE ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO
SEQRES 30 A 466 GLY PHE PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU
SEQRES 31 A 466 THR ALA GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO
SEQRES 32 A 466 VAL ALA GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA
SEQRES 33 A 466 TRP ARG ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU
SEQRES 34 A 466 HIS LYS GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY
SEQRES 35 A 466 ASP ALA ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU
SEQRES 36 A 466 GLY VAL GLU ASP THR ARG SER ALA LEU PRO ALA
SEQRES 1 B 466 MET ASP GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS
SEQRES 2 B 466 GLU GLU ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS
SEQRES 3 B 466 ALA TYR ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL
SEQRES 4 B 466 ALA THR ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY
SEQRES 5 B 466 THR ASN VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG
SEQRES 6 B 466 GLY VAL ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG
SEQRES 7 B 466 GLU LEU THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP
SEQRES 8 B 466 ARG ASN ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE
SEQRES 9 B 466 LEU THR LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP
SEQRES 10 B 466 VAL GLU TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU
SEQRES 11 B 466 ALA TYR ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE
SEQRES 12 B 466 SER ALA LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP
SEQRES 13 B 466 GLY GLY LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU
SEQRES 14 B 466 GLY LEU ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA
SEQRES 15 B 466 PHE TRP LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO
SEQRES 16 B 466 GLN GLY ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE
SEQRES 17 B 466 ALA LEU VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU
SEQRES 18 B 466 THR GLY GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA
SEQRES 19 B 466 ASP ASP PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL
SEQRES 20 B 466 LEU GLU THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU
SEQRES 21 B 466 LEU VAL ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR
SEQRES 22 B 466 THR ALA ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR
SEQRES 23 B 466 HIS ARG ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER
SEQRES 24 B 466 LYS ARG GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA
SEQRES 25 B 466 ARG LEU GLN GLY ALA SER GLY ILE HIS THR GLY THR MET
SEQRES 26 B 466 GLY PHE GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA
SEQRES 27 B 466 ILE ALA TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO
SEQRES 28 B 466 PHE TYR ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR
SEQRES 29 B 466 PRO ILE ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO
SEQRES 30 B 466 GLY PHE PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU
SEQRES 31 B 466 THR ALA GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO
SEQRES 32 B 466 VAL ALA GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA
SEQRES 33 B 466 TRP ARG ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU
SEQRES 34 B 466 HIS LYS GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY
SEQRES 35 B 466 ASP ALA ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU
SEQRES 36 B 466 GLY VAL GLU ASP THR ARG SER ALA LEU PRO ALA
HET RUB A 600 18
HET RUB B 700 18
HET MG A 500 1
HET MG B 500 1
HET FMT A 601 3
HET FMT B 701 3
HETNAM RUB RIBULOSE-1,5-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM FMT FORMIC ACID
FORMUL 3 RUB 2(C5 H12 O11 P2)
FORMUL 5 MG 2(MG 2+)
FORMUL 7 FMT 2(C H2 O2)
HELIX 1 AA GLU A 14 GLY A 20 1 7
HELIX 2 AB TYR A 38 SER A 49 1 12
HELIX 3 AC ILE A 101 MET A 109 1 9
HELIX 4 AD GLU A 130 ARG A 133 1 4
HELIX 5 AE SER A 144 LEU A 150 1 7
HELIX 6 A1 PRO A 173 TRP A 184 1 12
HELIX 7 A2 LEU A 204 THR A 222 1 19
HELIX 8 A3 ASP A 235 PHE A 251 1 17
HELIX 9 A4 ALA A 269 ARG A 278 1 10
HELIX 10 AF GLY A 292 THR A 295 1 4
HELIX 11 A5 ALA A 305 GLN A 315 1 11
HELIX 12 A6 ARG A 337 THR A 344 1 8
HELIX 13 A7 ARG A 375 GLY A 378 5 4
HELIX 14 A8 PRO A 403 ASP A 419 1 17
HELIX 15 AG VAL A 423 GLU A 429 1 7
HELIX 16 AH LYS A 431 PHE A 440 1 10
HELIX 17 AI GLY A 442 TYR A 448 1 7
HELIX 18 AJ TRP A 451 LEU A 455 1 5
HELIX 19 BA GLU B 14 GLY B 20 1 7
HELIX 20 BB TYR B 38 SER B 49 1 12
HELIX 21 BC ILE B 101 MET B 109 1 9
HELIX 22 BD GLU B 130 ARG B 133 1 4
HELIX 23 BE SER B 144 LEU B 150 1 7
HELIX 24 B1 PRO B 173 TRP B 184 1 12
HELIX 25 B2 LEU B 204 THR B 222 1 19
HELIX 26 B3 ASP B 235 PHE B 251 1 17
HELIX 27 B4 ALA B 269 ARG B 278 1 10
HELIX 28 BF GLY B 292 THR B 295 1 4
HELIX 29 B5 ALA B 305 GLN B 315 1 11
HELIX 30 B6 ARG B 337 THR B 344 1 8
HELIX 31 B6 ARG B 375 LEU B 383 1 9
HELIX 32 B8 PRO B 403 ASP B 419 1 17
HELIX 33 BG VAL B 423 GLU B 429 1 7
HELIX 34 BH LYS B 431 PHE B 440 1 10
HELIX 35 BI GLY B 442 TYR B 448 1 7
HELIX 36 BJ TRP B 451 LEU B 455 1 5
SHEET 1 ANT 5 VAL A 8 LEU A 10 0
SHEET 2 ANT 5 ALA A 69 ASP A 75 1
SHEET 3 ANT 5 GLU A 79 PRO A 86 -1
SHEET 4 ANT 5 HIS A 23 PRO A 32 -1
SHEET 5 ANT 5 ASP A 117 TYR A 127 -1
SHEET 1 CTA 9 VAL A 160 ILE A 164 0
SHEET 2 CTA 9 PHE A 189 LYS A 191 1
SHEET 3 CTA 9 LEU A 227 ASN A 231 1
SHEET 4 CTA 9 VAL A 258 ASP A 263 1
SHEET 5 CTA 9 LEU A 284 HIS A 287 1
SHEET 6 CTA 9 GLY A 319 HIS A 321 1
SHEET 7 CTA 9 THR A 364 GLY A 369 1
SHEET 8 CTA 9 ILE A 389 ALA A 392 1
SHEET 9 CTA 9 VAL A 160 ILE A 164 1
SHEET 1 BNT 5 VAL B 8 LEU B 10 0
SHEET 2 BNT 5 ALA B 69 ASP B 75 1
SHEET 3 BNT 5 GLU B 79 PRO B 86 -1
SHEET 4 BNT 5 HIS B 23 PRO B 32 -1
SHEET 5 BNT 5 ASP B 117 TYR B 127 -1
SHEET 1 CTB 9 VAL B 160 ILE B 164 0
SHEET 2 CTB 9 PHE B 189 LYS B 191 1
SHEET 3 CTB 9 LEU B 227 ASN B 231 1
SHEET 4 CTB 9 VAL B 258 ASP B 263 1
SHEET 5 CTB 9 LEU B 284 HIS B 287 1
SHEET 6 CTB 9 GLY B 319 HIS B 321 1
SHEET 7 CTB 9 THR B 364 GLY B 369 1
SHEET 8 CTB 9 ILE A 389 ALA A 392 1
SHEET 9 CTB 9 VAL B 160 ILE B 164 1
LINK NZ LYS A 191 C FMT A 601 1555 1555 1.45
LINK NZ LYS B 191 C FMT B 701 1555 1555 1.51
LINK MG MG A 500 O2 RUB A 600 1555 1555 2.47
LINK MG MG A 500 O3 RUB A 600 1555 1555 2.62
LINK MG MG A 500 OD1 ASP A 193 1555 1555 2.55
LINK MG MG A 500 O1 FMT A 601 1555 1555 2.39
LINK MG MG A 500 O2 FMT A 601 1555 1555 2.45
LINK MG MG B 500 O1 FMT B 701 1555 1555 2.46
LINK MG MG B 500 OD1 ASP B 193 1555 1555 2.53
LINK MG MG B 500 O3 RUB B 700 1555 1555 2.17
LINK MG MG B 500 O2 RUB B 700 1555 1555 2.42
LINK O3 RUB B 700 O2 FMT B 701 1555 1555 2.03
CISPEP 1 LYS A 166 PRO A 167 0 5.20
CISPEP 2 LYS B 166 PRO B 167 0 3.51
SITE 1 ACT 5 FMT A 601 LYS A 191 ASP A 193 GLU A 194
SITE 2 ACT 5 MG A 500
SITE 1 BCT 5 FMT B 701 LYS B 191 ASP B 193 GLU B 194
SITE 2 BCT 5 MG B 500
SITE 1 AC1 10 ILE A 164 ASP A 193 HIS A 321 ILE A 366
SITE 2 AC1 10 SER A 368 ALA A 392 GLY A 393 MG A 500
SITE 3 AC1 10 FMT A 601 ASN B 111
SITE 1 AC2 11 ILE B 164 HIS B 287 HIS B 321 THR B 322
SITE 2 AC2 11 SER B 368 GLY B 369 THR B 391 ALA B 392
SITE 3 AC2 11 GLY B 393 MG B 500 FMT B 701
SITE 1 AC3 3 ASP A 193 RUB A 600 FMT A 601
SITE 1 AC4 4 ASP B 193 GLU B 194 RUB B 700 FMT B 701
SITE 1 AC5 6 ILE A 164 LYS A 191 ASN A 192 ASP A 193
SITE 2 AC5 6 MG A 500 RUB A 600
SITE 1 AC6 7 LYS B 191 ASP B 193 GLU B 194 HIS B 287
SITE 2 AC6 7 HIS B 321 MG B 500 RUB B 700
CRYST1 65.500 70.600 104.100 90.00 92.10 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.036668 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000672 0.00000
SCALE1 0.015267 0.000000 0.000560 0.00000
SCALE2 0.000000 0.014164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009613 0.00000
MTRIX1 1 0.373740 -0.056007 0.940855 6.14161 1
MTRIX2 1 -0.073400 -0.996800 -0.033512 17.87800 1
MTRIX3 1 0.909789 -0.054363 -0.376740 -7.57091 1
(ATOM LINES ARE NOT SHOWN.)
END
