HEADER LYASE 07-AUG-01 1JQO
TITLE CRYSTAL STRUCTURE OF C4-FORM PHOSPHOENOLPYRUVATE CARBOXYLASE FROM
TITLE 2 MAIZE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOENOLPYRUVATE CARBOXYLASE 1, PEPCASE;
COMPND 5 EC: 4.1.1.31
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_TAXID: 4577;
SOURCE 4 STRAIN: B37;
SOURCE 5 TISSUE: LEAVES
KEYWDS BETA BARREL, CARBON DIOXIDE FIXATION, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MATSUMURA,Y.KAI
REVDAT 4 13-MAR-24 1JQO 1 REMARK
REVDAT 3 13-JUL-11 1JQO 1 VERSN
REVDAT 2 24-FEB-09 1JQO 1 VERSN
REVDAT 1 14-JAN-03 1JQO 0
JRNL AUTH H.MATSUMURA,Y.XIE,S.SHIRAKATA,T.INOUE,T.YOSHINAGA,Y.UENO,
JRNL AUTH 2 K.IZUI,Y.KAI
JRNL TITL CRYSTAL STRUCTURES OF C4 FORM MAIZE AND QUATERNARY COMPLEX
JRNL TITL 2 OF E. COLI PHOSPHOENOLPYRUVATE CARBOXYLASES.
JRNL REF STRUCTURE V. 10 1721 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12467579
JRNL DOI 10.1016/S0969-2126(02)00913-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.MATSUMURA,M.TERADA,S.SHIRAKATA,T.INOUE,T.YOSHINAGA,K.IZUI,
REMARK 1 AUTH 2 Y.KAI
REMARK 1 TITL PLAUSIBLE PHOSPHOENOLPYRUVATE BINDING SITE REVEALED BY 2.6 A
REMARK 1 TITL 2 STRUCTURE OF MN2+-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE FROM
REMARK 1 TITL 3 ESCHERICHIA COLI.
REMARK 1 REF FEBS LETT. V. 458 93 1999
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.KAI,H.MATSUMURA,T.INOUE,K.TERADA,Y.NAGARA,T.YOSHINAGA,
REMARK 1 AUTH 2 A.KIHARA,K.TSUMURA,K.IZUI
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE
REMARK 1 TITL 2 CARBOXYLASE: A PROPOSED MECHANISM FOR ALLOSTERIC INHIBITION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 96 823 1999
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.MATSUMURA,T.NAGATA,M.TERADA,S.SHIRAKATA,T.INOUE,
REMARK 1 AUTH 2 T.YOSHINAGA,Y.UENO,H.SAZE,K.IZUI,Y.KAI
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK 1 TITL 2 C4-FORM PHOSPHOENOLPYRUVATE CARBOXYLASE FROM MAIZE
REMARK 1 TITL 3 DIFFRACTION STUDIES OF C4-FORM PHOSPHOENOLPYRUVATE
REMARK 1 TITL 4 CARBOXYLASE FROM MAIZE.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 1937 1999
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 57271
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 SET) : 0.236
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2893
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4130
REMARK 3 BIN FREE R VALUE : 0.4150
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14424
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
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) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : 1.06
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.708
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58078
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 86.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 7.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09100
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) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30900
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, TRIS-HCL, LISO4, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 127.14000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 127.14000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 79.22000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 87.30500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 79.22000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 87.30500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 127.14000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 79.22000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 87.30500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 127.14000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 79.22000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 87.30500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: THE BIOLOGICAL ASSEMBLY IS A TETRAMER GENERATED FROM DIMER
REMARK 300 IN THE ASSYMMETRIC UNIT BY TWO FOLE AXIS.
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: TETRAMERIC
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 174.61000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 254.28000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 ALA A 2
REMARK 465 SER A 3
REMARK 465 THR A 4
REMARK 465 LYS A 5
REMARK 465 ALA A 6
REMARK 465 PRO A 7
REMARK 465 GLY A 8
REMARK 465 PRO A 9
REMARK 465 GLY A 10
REMARK 465 GLU A 11
REMARK 465 LYS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 SER A 15
REMARK 465 ILE A 16
REMARK 465 ASP A 17
REMARK 465 ALA A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ARG A 21
REMARK 465 GLN A 22
REMARK 465 LEU A 23
REMARK 465 VAL A 24
REMARK 465 PRO A 25
REMARK 465 GLY A 26
REMARK 465 LYS A 27
REMARK 465 VAL A 28
REMARK 465 SER A 29
REMARK 465 GLU A 30
REMARK 465 ASP A 31
REMARK 465 ASP A 32
REMARK 465 LYS A 33
REMARK 465 LEU A 34
REMARK 465 SER A 124
REMARK 465 LYS A 125
REMARK 465 LEU A 126
REMARK 465 LYS A 127
REMARK 465 LYS A 128
REMARK 465 GLY A 129
REMARK 465 GLY A 130
REMARK 465 PHE A 131
REMARK 465 ALA A 132
REMARK 465 ASP A 133
REMARK 465 GLU A 134
REMARK 465 GLY A 135
REMARK 465 SER A 136
REMARK 465 ALA A 137
REMARK 465 THR A 138
REMARK 465 THR A 139
REMARK 465 GLU A 140
REMARK 465 ALA A 761
REMARK 465 LYS A 762
REMARK 465 ARG A 763
REMARK 465 ARG A 764
REMARK 465 PRO A 765
REMARK 465 GLY A 766
REMARK 465 GLY A 767
REMARK 465 GLY A 768
REMARK 465 PHE A 929
REMARK 465 ALA A 930
REMARK 465 ASP A 931
REMARK 465 GLU A 932
REMARK 465 ASN A 933
REMARK 465 LYS A 934
REMARK 465 PRO A 935
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 THR B 4
REMARK 465 LYS B 5
REMARK 465 ALA B 6
REMARK 465 PRO B 7
REMARK 465 GLY B 8
REMARK 465 PRO B 9
REMARK 465 GLY B 10
REMARK 465 GLU B 11
REMARK 465 LYS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 SER B 15
REMARK 465 ILE B 16
REMARK 465 ASP B 17
REMARK 465 ALA B 18
REMARK 465 GLN B 19
REMARK 465 LEU B 20
REMARK 465 ARG B 21
REMARK 465 GLN B 22
REMARK 465 LEU B 23
REMARK 465 VAL B 24
REMARK 465 PRO B 25
REMARK 465 GLY B 26
REMARK 465 LYS B 27
REMARK 465 VAL B 28
REMARK 465 SER B 29
REMARK 465 GLU B 30
REMARK 465 ASP B 31
REMARK 465 ASP B 32
REMARK 465 LYS B 33
REMARK 465 LEU B 34
REMARK 465 SER B 124
REMARK 465 LYS B 125
REMARK 465 LEU B 126
REMARK 465 LYS B 127
REMARK 465 LYS B 128
REMARK 465 GLY B 129
REMARK 465 GLY B 130
REMARK 465 PHE B 131
REMARK 465 ALA B 132
REMARK 465 ASP B 133
REMARK 465 GLU B 134
REMARK 465 GLY B 135
REMARK 465 SER B 136
REMARK 465 ALA B 137
REMARK 465 THR B 138
REMARK 465 THR B 139
REMARK 465 GLU B 140
REMARK 465 ALA B 761
REMARK 465 LYS B 762
REMARK 465 ARG B 763
REMARK 465 ARG B 764
REMARK 465 PRO B 765
REMARK 465 GLY B 766
REMARK 465 GLY B 767
REMARK 465 GLY B 768
REMARK 465 PHE B 929
REMARK 465 ALA B 930
REMARK 465 ASP B 931
REMARK 465 GLU B 932
REMARK 465 ASN B 933
REMARK 465 LYS B 934
REMARK 465 PRO B 935
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 PRO A 55 C - N - CA ANGL. DEV. = 9.5 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 ARG A 120 -76.09 -45.16
REMARK 500 SER A 152 -82.40 -77.64
REMARK 500 GLU A 153 -71.71 -50.55
REMARK 500 ALA A 176 52.81 -97.74
REMARK 500 PRO A 178 62.13 -59.28
REMARK 500 THR A 206 -172.01 -61.82
REMARK 500 HIS A 249 35.38 -91.14
REMARK 500 GLU A 250 -24.05 -146.99
REMARK 500 THR A 251 -37.90 -143.50
REMARK 500 ILE A 272 96.05 -50.85
REMARK 500 ASN A 273 47.28 -84.41
REMARK 500 MET A 289 95.04 -67.17
REMARK 500 SER A 331 32.31 -87.72
REMARK 500 ARG A 334 98.49 -68.54
REMARK 500 SER A 350 -70.56 -68.51
REMARK 500 LYS A 353 -3.99 -144.77
REMARK 500 VAL A 354 10.50 -64.33
REMARK 500 PRO A 367 4.00 -69.37
REMARK 500 GLU A 369 74.56 -119.24
REMARK 500 ALA A 394 -72.72 -59.48
REMARK 500 SER A 395 -149.53 -92.58
REMARK 500 CYS A 426 24.52 -75.06
REMARK 500 ASP A 428 69.43 -45.47
REMARK 500 ASP A 433 9.76 -68.53
REMARK 500 LEU A 450 -50.21 -21.92
REMARK 500 GLN A 457 126.26 -173.41
REMARK 500 ILE A 475 43.36 -150.60
REMARK 500 GLU A 480 10.66 -65.68
REMARK 500 LYS A 497 -16.81 -149.28
REMARK 500 SER A 528 9.04 -64.15
REMARK 500 MET A 536 42.61 35.38
REMARK 500 THR A 538 -90.46 -102.66
REMARK 500 LEU A 548 -71.15 -72.19
REMARK 500 ARG A 556 -81.24 -43.00
REMARK 500 GLU A 566 -53.93 -132.65
REMARK 500 SER A 573 31.31 -73.89
REMARK 500 ALA A 576 -71.46 -67.69
REMARK 500 PRO A 660 139.33 -39.68
REMARK 500 ILE A 664 -61.07 -122.90
REMARK 500 GLU A 684 -79.89 -65.24
REMARK 500 HIS A 704 65.04 -154.14
REMARK 500 PRO A 705 159.76 -49.91
REMARK 500 TYR A 728 -74.83 -62.48
REMARK 500 VAL A 733 -64.38 -107.95
REMARK 500 ARG A 737 8.64 -65.11
REMARK 500 PRO A 747 36.47 -90.53
REMARK 500 ARG A 773 144.68 1.24
REMARK 500 VAL A 794 -36.65 -25.21
REMARK 500 ASP A 837 100.11 -166.33
REMARK 500 ASN A 895 -53.92 -27.55
REMARK 500
REMARK 500 THIS ENTRY HAS 118 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 971
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1071
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FIY RELATED DB: PDB
REMARK 900 1FIY CONTAINS THE NATIVE STRUCTURE OF E.COLI PEPC.
REMARK 900 RELATED ID: 1JQN RELATED DB: PDB
REMARK 900 1JQN CONTAINS STRUCTURE OF E.COLI PHOSPHOENOLPYRUVATE CARBOXYLASE
REMARK 900 IN COMPLEX WITH MN2+ AND DCDP
DBREF 1JQO A 1 970 UNP P04711 CAPP1_MAIZE 1 970
DBREF 1JQO B 1 970 UNP P04711 CAPP1_MAIZE 1 970
SEQRES 1 A 970 MET ALA SER THR LYS ALA PRO GLY PRO GLY GLU LYS HIS
SEQRES 2 A 970 HIS SER ILE ASP ALA GLN LEU ARG GLN LEU VAL PRO GLY
SEQRES 3 A 970 LYS VAL SER GLU ASP ASP LYS LEU ILE GLU TYR ASP ALA
SEQRES 4 A 970 LEU LEU VAL ASP ARG PHE LEU ASN ILE LEU GLN ASP LEU
SEQRES 5 A 970 HIS GLY PRO SER LEU ARG GLU PHE VAL GLN GLU CYS TYR
SEQRES 6 A 970 GLU VAL SER ALA ASP TYR GLU GLY LYS GLY ASP THR THR
SEQRES 7 A 970 LYS LEU GLY GLU LEU GLY ALA LYS LEU THR GLY LEU ALA
SEQRES 8 A 970 PRO ALA ASP ALA ILE LEU VAL ALA SER SER ILE LEU HIS
SEQRES 9 A 970 MET LEU ASN LEU ALA ASN LEU ALA GLU GLU VAL GLN ILE
SEQRES 10 A 970 ALA HIS ARG ARG ARG ASN SER LYS LEU LYS LYS GLY GLY
SEQRES 11 A 970 PHE ALA ASP GLU GLY SER ALA THR THR GLU SER ASP ILE
SEQRES 12 A 970 GLU GLU THR LEU LYS ARG LEU VAL SER GLU VAL GLY LYS
SEQRES 13 A 970 SER PRO GLU GLU VAL PHE GLU ALA LEU LYS ASN GLN THR
SEQRES 14 A 970 VAL ASP LEU VAL PHE THR ALA HIS PRO THR GLN SER ALA
SEQRES 15 A 970 ARG ARG SER LEU LEU GLN LYS ASN ALA ARG ILE ARG ASN
SEQRES 16 A 970 CYS LEU THR GLN LEU ASN ALA LYS ASP ILE THR ASP ASP
SEQRES 17 A 970 ASP LYS GLN GLU LEU ASP GLU ALA LEU GLN ARG GLU ILE
SEQRES 18 A 970 GLN ALA ALA PHE ARG THR ASP GLU ILE ARG ARG ALA GLN
SEQRES 19 A 970 PRO THR PRO GLN ALA GLU MET ARG TYR GLY MET SER TYR
SEQRES 20 A 970 ILE HIS GLU THR VAL TRP LYS GLY VAL PRO LYS PHE LEU
SEQRES 21 A 970 ARG ARG VAL ASP THR ALA LEU LYS ASN ILE GLY ILE ASN
SEQRES 22 A 970 GLU ARG LEU PRO TYR ASN VAL SER LEU ILE ARG PHE SER
SEQRES 23 A 970 SER TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ARG VAL
SEQRES 24 A 970 THR PRO GLU VAL THR ARG ASP VAL CYS LEU LEU ALA ARG
SEQRES 25 A 970 MET MET ALA ALA ASN LEU TYR ILE ASP GLN ILE GLU GLU
SEQRES 26 A 970 LEU MET PHE GLU LEU SER MET TRP ARG CYS ASN ASP GLU
SEQRES 27 A 970 LEU ARG VAL ARG ALA GLU GLU LEU HIS SER SER SER GLY
SEQRES 28 A 970 SER LYS VAL THR LYS TYR TYR ILE GLU PHE TRP LYS GLN
SEQRES 29 A 970 ILE PRO PRO ASN GLU PRO TYR ARG VAL ILE LEU GLY HIS
SEQRES 30 A 970 VAL ARG ASP LYS LEU TYR ASN THR ARG GLU ARG ALA ARG
SEQRES 31 A 970 HIS LEU LEU ALA SER GLY VAL SER GLU ILE SER ALA GLU
SEQRES 32 A 970 SER SER PHE THR SER ILE GLU GLU PHE LEU GLU PRO LEU
SEQRES 33 A 970 GLU LEU CYS TYR LYS SER LEU CYS ASP CYS GLY ASP LYS
SEQRES 34 A 970 ALA ILE ALA ASP GLY SER LEU LEU ASP LEU LEU ARG GLN
SEQRES 35 A 970 VAL PHE THR PHE GLY LEU SER LEU VAL LYS LEU ASP ILE
SEQRES 36 A 970 ARG GLN GLU SER GLU ARG HIS THR ASP VAL ILE ASP ALA
SEQRES 37 A 970 ILE THR THR HIS LEU GLY ILE GLY SER TYR ARG GLU TRP
SEQRES 38 A 970 PRO GLU ASP LYS ARG GLN GLU TRP LEU LEU SER GLU LEU
SEQRES 39 A 970 ARG GLY LYS ARG PRO LEU LEU PRO PRO ASP LEU PRO GLN
SEQRES 40 A 970 THR ASP GLU ILE ALA ASP VAL ILE GLY ALA PHE HIS VAL
SEQRES 41 A 970 LEU ALA GLU LEU PRO PRO ASP SER PHE GLY PRO TYR ILE
SEQRES 42 A 970 ILE SER MET ALA THR ALA PRO SER ASP VAL LEU ALA VAL
SEQRES 43 A 970 GLU LEU LEU GLN ARG GLU CYS GLY VAL ARG GLN PRO LEU
SEQRES 44 A 970 PRO VAL VAL PRO LEU PHE GLU ARG LEU ALA ASP LEU GLN
SEQRES 45 A 970 SER ALA PRO ALA SER VAL GLU ARG LEU PHE SER VAL ASP
SEQRES 46 A 970 TRP TYR MET ASP ARG ILE LYS GLY LYS GLN GLN VAL MET
SEQRES 47 A 970 VAL GLY TYR SER ASP SER GLY LYS ASP ALA GLY ARG LEU
SEQRES 48 A 970 SER ALA ALA TRP GLN LEU TYR ARG ALA GLN GLU GLU MET
SEQRES 49 A 970 ALA GLN VAL ALA LYS ARG TYR GLY VAL LYS LEU THR LEU
SEQRES 50 A 970 PHE HIS GLY ARG GLY GLY THR VAL GLY ARG GLY GLY GLY
SEQRES 51 A 970 PRO THR HIS LEU ALA ILE LEU SER GLN PRO PRO ASP THR
SEQRES 52 A 970 ILE ASN GLY SER ILE ARG VAL THR VAL GLN GLY GLU VAL
SEQRES 53 A 970 ILE GLU PHE CYS PHE GLY GLU GLU HIS LEU CYS PHE GLN
SEQRES 54 A 970 THR LEU GLN ARG PHE THR ALA ALA THR LEU GLU HIS GLY
SEQRES 55 A 970 MET HIS PRO PRO VAL SER PRO LYS PRO GLU TRP ARG LYS
SEQRES 56 A 970 LEU MET ASP GLU MET ALA VAL VAL ALA THR GLU GLU TYR
SEQRES 57 A 970 ARG SER VAL VAL VAL LYS GLU ALA ARG PHE VAL GLU TYR
SEQRES 58 A 970 PHE ARG SER ALA THR PRO GLU THR GLU TYR GLY ARG MET
SEQRES 59 A 970 ASN ILE GLY SER ARG PRO ALA LYS ARG ARG PRO GLY GLY
SEQRES 60 A 970 GLY ILE THR THR LEU ARG ALA ILE PRO TRP ILE PHE SER
SEQRES 61 A 970 TRP THR GLN THR ARG PHE HIS LEU PRO VAL TRP LEU GLY
SEQRES 62 A 970 VAL GLY ALA ALA PHE LYS PHE ALA ILE ASP LYS ASP VAL
SEQRES 63 A 970 ARG ASN PHE GLN VAL LEU LYS GLU MET TYR ASN GLU TRP
SEQRES 64 A 970 PRO PHE PHE ARG VAL THR LEU ASP LEU LEU GLU MET VAL
SEQRES 65 A 970 PHE ALA LYS GLY ASP PRO GLY ILE ALA GLY LEU TYR ASP
SEQRES 66 A 970 GLU LEU LEU VAL ALA GLU GLU LEU LYS PRO PHE GLY LYS
SEQRES 67 A 970 GLN LEU ARG ASP LYS TYR VAL GLU THR GLN GLN LEU LEU
SEQRES 68 A 970 LEU GLN ILE ALA GLY HIS LYS ASP ILE LEU GLU GLY ASP
SEQRES 69 A 970 PRO PHE LEU LYS GLN GLY LEU VAL LEU ARG ASN PRO TYR
SEQRES 70 A 970 ILE THR THR LEU ASN VAL PHE GLN ALA TYR THR LEU LYS
SEQRES 71 A 970 ARG ILE ARG ASP PRO ASN PHE LYS VAL THR PRO GLN PRO
SEQRES 72 A 970 PRO LEU SER LYS GLU PHE ALA ASP GLU ASN LYS PRO ALA
SEQRES 73 A 970 GLY LEU VAL LYS LEU ASN PRO ALA SER GLU TYR PRO PRO
SEQRES 74 A 970 GLY LEU GLU ASP THR LEU ILE LEU THR MET LYS GLY ILE
SEQRES 75 A 970 ALA ALA GLY MET GLN ASN THR GLY
SEQRES 1 B 970 MET ALA SER THR LYS ALA PRO GLY PRO GLY GLU LYS HIS
SEQRES 2 B 970 HIS SER ILE ASP ALA GLN LEU ARG GLN LEU VAL PRO GLY
SEQRES 3 B 970 LYS VAL SER GLU ASP ASP LYS LEU ILE GLU TYR ASP ALA
SEQRES 4 B 970 LEU LEU VAL ASP ARG PHE LEU ASN ILE LEU GLN ASP LEU
SEQRES 5 B 970 HIS GLY PRO SER LEU ARG GLU PHE VAL GLN GLU CYS TYR
SEQRES 6 B 970 GLU VAL SER ALA ASP TYR GLU GLY LYS GLY ASP THR THR
SEQRES 7 B 970 LYS LEU GLY GLU LEU GLY ALA LYS LEU THR GLY LEU ALA
SEQRES 8 B 970 PRO ALA ASP ALA ILE LEU VAL ALA SER SER ILE LEU HIS
SEQRES 9 B 970 MET LEU ASN LEU ALA ASN LEU ALA GLU GLU VAL GLN ILE
SEQRES 10 B 970 ALA HIS ARG ARG ARG ASN SER LYS LEU LYS LYS GLY GLY
SEQRES 11 B 970 PHE ALA ASP GLU GLY SER ALA THR THR GLU SER ASP ILE
SEQRES 12 B 970 GLU GLU THR LEU LYS ARG LEU VAL SER GLU VAL GLY LYS
SEQRES 13 B 970 SER PRO GLU GLU VAL PHE GLU ALA LEU LYS ASN GLN THR
SEQRES 14 B 970 VAL ASP LEU VAL PHE THR ALA HIS PRO THR GLN SER ALA
SEQRES 15 B 970 ARG ARG SER LEU LEU GLN LYS ASN ALA ARG ILE ARG ASN
SEQRES 16 B 970 CYS LEU THR GLN LEU ASN ALA LYS ASP ILE THR ASP ASP
SEQRES 17 B 970 ASP LYS GLN GLU LEU ASP GLU ALA LEU GLN ARG GLU ILE
SEQRES 18 B 970 GLN ALA ALA PHE ARG THR ASP GLU ILE ARG ARG ALA GLN
SEQRES 19 B 970 PRO THR PRO GLN ALA GLU MET ARG TYR GLY MET SER TYR
SEQRES 20 B 970 ILE HIS GLU THR VAL TRP LYS GLY VAL PRO LYS PHE LEU
SEQRES 21 B 970 ARG ARG VAL ASP THR ALA LEU LYS ASN ILE GLY ILE ASN
SEQRES 22 B 970 GLU ARG LEU PRO TYR ASN VAL SER LEU ILE ARG PHE SER
SEQRES 23 B 970 SER TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ARG VAL
SEQRES 24 B 970 THR PRO GLU VAL THR ARG ASP VAL CYS LEU LEU ALA ARG
SEQRES 25 B 970 MET MET ALA ALA ASN LEU TYR ILE ASP GLN ILE GLU GLU
SEQRES 26 B 970 LEU MET PHE GLU LEU SER MET TRP ARG CYS ASN ASP GLU
SEQRES 27 B 970 LEU ARG VAL ARG ALA GLU GLU LEU HIS SER SER SER GLY
SEQRES 28 B 970 SER LYS VAL THR LYS TYR TYR ILE GLU PHE TRP LYS GLN
SEQRES 29 B 970 ILE PRO PRO ASN GLU PRO TYR ARG VAL ILE LEU GLY HIS
SEQRES 30 B 970 VAL ARG ASP LYS LEU TYR ASN THR ARG GLU ARG ALA ARG
SEQRES 31 B 970 HIS LEU LEU ALA SER GLY VAL SER GLU ILE SER ALA GLU
SEQRES 32 B 970 SER SER PHE THR SER ILE GLU GLU PHE LEU GLU PRO LEU
SEQRES 33 B 970 GLU LEU CYS TYR LYS SER LEU CYS ASP CYS GLY ASP LYS
SEQRES 34 B 970 ALA ILE ALA ASP GLY SER LEU LEU ASP LEU LEU ARG GLN
SEQRES 35 B 970 VAL PHE THR PHE GLY LEU SER LEU VAL LYS LEU ASP ILE
SEQRES 36 B 970 ARG GLN GLU SER GLU ARG HIS THR ASP VAL ILE ASP ALA
SEQRES 37 B 970 ILE THR THR HIS LEU GLY ILE GLY SER TYR ARG GLU TRP
SEQRES 38 B 970 PRO GLU ASP LYS ARG GLN GLU TRP LEU LEU SER GLU LEU
SEQRES 39 B 970 ARG GLY LYS ARG PRO LEU LEU PRO PRO ASP LEU PRO GLN
SEQRES 40 B 970 THR ASP GLU ILE ALA ASP VAL ILE GLY ALA PHE HIS VAL
SEQRES 41 B 970 LEU ALA GLU LEU PRO PRO ASP SER PHE GLY PRO TYR ILE
SEQRES 42 B 970 ILE SER MET ALA THR ALA PRO SER ASP VAL LEU ALA VAL
SEQRES 43 B 970 GLU LEU LEU GLN ARG GLU CYS GLY VAL ARG GLN PRO LEU
SEQRES 44 B 970 PRO VAL VAL PRO LEU PHE GLU ARG LEU ALA ASP LEU GLN
SEQRES 45 B 970 SER ALA PRO ALA SER VAL GLU ARG LEU PHE SER VAL ASP
SEQRES 46 B 970 TRP TYR MET ASP ARG ILE LYS GLY LYS GLN GLN VAL MET
SEQRES 47 B 970 VAL GLY TYR SER ASP SER GLY LYS ASP ALA GLY ARG LEU
SEQRES 48 B 970 SER ALA ALA TRP GLN LEU TYR ARG ALA GLN GLU GLU MET
SEQRES 49 B 970 ALA GLN VAL ALA LYS ARG TYR GLY VAL LYS LEU THR LEU
SEQRES 50 B 970 PHE HIS GLY ARG GLY GLY THR VAL GLY ARG GLY GLY GLY
SEQRES 51 B 970 PRO THR HIS LEU ALA ILE LEU SER GLN PRO PRO ASP THR
SEQRES 52 B 970 ILE ASN GLY SER ILE ARG VAL THR VAL GLN GLY GLU VAL
SEQRES 53 B 970 ILE GLU PHE CYS PHE GLY GLU GLU HIS LEU CYS PHE GLN
SEQRES 54 B 970 THR LEU GLN ARG PHE THR ALA ALA THR LEU GLU HIS GLY
SEQRES 55 B 970 MET HIS PRO PRO VAL SER PRO LYS PRO GLU TRP ARG LYS
SEQRES 56 B 970 LEU MET ASP GLU MET ALA VAL VAL ALA THR GLU GLU TYR
SEQRES 57 B 970 ARG SER VAL VAL VAL LYS GLU ALA ARG PHE VAL GLU TYR
SEQRES 58 B 970 PHE ARG SER ALA THR PRO GLU THR GLU TYR GLY ARG MET
SEQRES 59 B 970 ASN ILE GLY SER ARG PRO ALA LYS ARG ARG PRO GLY GLY
SEQRES 60 B 970 GLY ILE THR THR LEU ARG ALA ILE PRO TRP ILE PHE SER
SEQRES 61 B 970 TRP THR GLN THR ARG PHE HIS LEU PRO VAL TRP LEU GLY
SEQRES 62 B 970 VAL GLY ALA ALA PHE LYS PHE ALA ILE ASP LYS ASP VAL
SEQRES 63 B 970 ARG ASN PHE GLN VAL LEU LYS GLU MET TYR ASN GLU TRP
SEQRES 64 B 970 PRO PHE PHE ARG VAL THR LEU ASP LEU LEU GLU MET VAL
SEQRES 65 B 970 PHE ALA LYS GLY ASP PRO GLY ILE ALA GLY LEU TYR ASP
SEQRES 66 B 970 GLU LEU LEU VAL ALA GLU GLU LEU LYS PRO PHE GLY LYS
SEQRES 67 B 970 GLN LEU ARG ASP LYS TYR VAL GLU THR GLN GLN LEU LEU
SEQRES 68 B 970 LEU GLN ILE ALA GLY HIS LYS ASP ILE LEU GLU GLY ASP
SEQRES 69 B 970 PRO PHE LEU LYS GLN GLY LEU VAL LEU ARG ASN PRO TYR
SEQRES 70 B 970 ILE THR THR LEU ASN VAL PHE GLN ALA TYR THR LEU LYS
SEQRES 71 B 970 ARG ILE ARG ASP PRO ASN PHE LYS VAL THR PRO GLN PRO
SEQRES 72 B 970 PRO LEU SER LYS GLU PHE ALA ASP GLU ASN LYS PRO ALA
SEQRES 73 B 970 GLY LEU VAL LYS LEU ASN PRO ALA SER GLU TYR PRO PRO
SEQRES 74 B 970 GLY LEU GLU ASP THR LEU ILE LEU THR MET LYS GLY ILE
SEQRES 75 B 970 ALA ALA GLY MET GLN ASN THR GLY
HET SO4 A 971 5
HET SO4 B1071 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
HELIX 1 1 ILE A 35 GLY A 54 1 20
HELIX 2 2 GLY A 54 GLY A 73 1 20
HELIX 3 3 THR A 77 LEU A 90 1 14
HELIX 4 4 ALA A 91 ASN A 123 1 33
HELIX 5 5 ASP A 142 SER A 152 1 11
HELIX 6 6 SER A 157 ASN A 167 1 11
HELIX 7 7 ARG A 183 LEU A 200 1 18
HELIX 8 8 THR A 206 THR A 227 1 22
HELIX 9 9 THR A 236 HIS A 249 1 14
HELIX 10 10 GLY A 255 ASN A 269 1 15
HELIX 11 11 THR A 300 LEU A 330 1 31
HELIX 12 12 ASN A 336 GLY A 351 1 16
HELIX 13 13 GLU A 369 SER A 395 1 27
HELIX 14 14 SER A 408 CYS A 426 1 19
HELIX 15 15 GLY A 434 GLY A 447 1 14
HELIX 16 16 GLU A 458 GLY A 474 1 17
HELIX 17 17 PRO A 482 GLY A 496 1 15
HELIX 18 18 THR A 508 LEU A 524 1 17
HELIX 19 19 PRO A 540 CYS A 553 1 14
HELIX 20 20 ARG A 567 SER A 573 1 7
HELIX 21 21 SER A 573 SER A 583 1 11
HELIX 22 22 VAL A 584 LYS A 592 1 9
HELIX 23 23 ASP A 603 ALA A 608 1 6
HELIX 24 24 GLY A 609 ARG A 630 1 22
HELIX 25 25 THR A 644 GLY A 648 5 5
HELIX 26 26 PRO A 651 SER A 658 1 8
HELIX 27 27 GLY A 674 GLY A 682 1 9
HELIX 28 28 GLU A 683 HIS A 704 1 22
HELIX 29 29 LYS A 710 VAL A 733 1 24
HELIX 30 30 ARG A 737 THR A 746 1 10
HELIX 31 31 GLU A 748 ASN A 755 5 8
HELIX 32 32 ALA A 774 THR A 784 1 11
HELIX 33 33 HIS A 787 LEU A 792 1 6
HELIX 34 34 GLY A 793 ASP A 805 1 13
HELIX 35 35 ARG A 807 TRP A 819 1 13
HELIX 36 36 TRP A 819 ALA A 834 1 16
HELIX 37 37 ASP A 837 LEU A 848 1 12
HELIX 38 38 LEU A 853 GLY A 876 1 24
HELIX 39 39 ASP A 884 ASP A 914 1 31
HELIX 40 40 GLY A 950 GLN A 967 1 18
HELIX 41 41 GLU B 36 GLY B 54 1 19
HELIX 42 42 GLY B 54 GLY B 73 1 20
HELIX 43 43 ASP B 76 GLY B 89 1 14
HELIX 44 44 ALA B 91 ARG B 122 1 32
HELIX 45 45 ASP B 142 SER B 152 1 11
HELIX 46 46 SER B 157 ASN B 167 1 11
HELIX 47 47 ARG B 183 LEU B 200 1 18
HELIX 48 48 THR B 206 ARG B 226 1 21
HELIX 49 49 THR B 236 THR B 251 1 16
HELIX 50 50 THR B 251 ASN B 269 1 19
HELIX 51 51 THR B 300 LEU B 330 1 31
HELIX 52 52 ASN B 336 SER B 349 1 14
HELIX 53 53 GLU B 369 SER B 395 1 27
HELIX 54 54 SER B 408 CYS B 426 1 19
HELIX 55 55 ASP B 428 ASP B 433 1 6
HELIX 56 56 GLY B 434 GLY B 447 1 14
HELIX 57 57 SER B 459 HIS B 472 1 14
HELIX 58 58 PRO B 482 GLY B 496 1 15
HELIX 59 59 THR B 508 LEU B 524 1 17
HELIX 60 60 PRO B 525 ASP B 527 5 3
HELIX 61 61 ALA B 539 GLU B 552 1 14
HELIX 62 62 ARG B 567 PHE B 582 1 16
HELIX 63 63 VAL B 584 LYS B 592 1 9
HELIX 64 64 ASP B 603 ALA B 608 1 6
HELIX 65 65 GLY B 609 TYR B 631 1 23
HELIX 66 66 THR B 644 GLY B 648 5 5
HELIX 67 67 PRO B 651 SER B 658 1 8
HELIX 68 68 GLY B 674 GLY B 682 1 9
HELIX 69 69 GLU B 683 HIS B 704 1 22
HELIX 70 70 LYS B 710 VAL B 733 1 24
HELIX 71 71 GLU B 735 THR B 746 1 12
HELIX 72 72 PRO B 747 ASN B 755 5 9
HELIX 73 73 ARG B 773 THR B 784 1 12
HELIX 74 74 HIS B 787 LEU B 792 1 6
HELIX 75 75 GLY B 793 LYS B 804 1 12
HELIX 76 76 VAL B 806 TRP B 819 1 14
HELIX 77 77 TRP B 819 ALA B 834 1 16
HELIX 78 78 ASP B 837 TYR B 844 1 8
HELIX 79 79 TYR B 844 VAL B 849 1 6
HELIX 80 80 LEU B 853 GLY B 876 1 24
HELIX 81 81 ASP B 884 ASP B 914 1 31
HELIX 82 82 LEU B 938 ASN B 942 5 5
HELIX 83 83 GLY B 950 GLN B 967 1 18
SHEET 1 A 9 THR A 169 THR A 175 0
SHEET 2 A 9 ILE A 283 SER A 287 1 O ARG A 284 N LEU A 172
SHEET 3 A 9 LYS A 452 ARG A 456 1 O ASP A 454 N SER A 287
SHEET 4 A 9 PHE A 529 ILE A 534 1 O ILE A 533 N ILE A 455
SHEET 5 A 9 VAL A 561 PHE A 565 1 O VAL A 562 N ILE A 534
SHEET 6 A 9 LYS A 594 GLY A 600 1 O GLY A 600 N PHE A 565
SHEET 7 A 9 LYS A 634 GLY A 640 1 O PHE A 638 N VAL A 599
SHEET 8 A 9 SER A 667 GLN A 673 1 O ARG A 669 N HIS A 639
SHEET 9 A 9 THR A 169 THR A 175 1 N VAL A 173 O VAL A 672
SHEET 1 B 9 THR B 169 THR B 175 0
SHEET 2 B 9 ILE B 283 SER B 287 1 O SER B 286 N PHE B 174
SHEET 3 B 9 LYS B 452 GLU B 458 1 O LYS B 452 N SER B 287
SHEET 4 B 9 PHE B 529 SER B 535 1 O GLY B 530 N LEU B 453
SHEET 5 B 9 VAL B 561 PHE B 565 1 O VAL B 562 N TYR B 532
SHEET 6 B 9 LYS B 594 GLY B 600 1 O MET B 598 N PHE B 565
SHEET 7 B 9 LYS B 634 GLY B 640 1 O PHE B 638 N VAL B 599
SHEET 8 B 9 SER B 667 GLN B 673 1 O ARG B 669 N HIS B 639
SHEET 9 B 9 THR B 169 THR B 175 1 N VAL B 173 O VAL B 670
SITE 1 AC1 4 ARG A 183 ARG A 184 SER A 185 ARG A 231
SITE 1 AC2 4 ARG B 183 ARG B 184 SER B 185 ARG B 231
CRYST1 158.440 174.610 254.280 90.00 90.00 90.00 C 2 2 21 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 0.006312 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003933 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
