HEADER LIGASE 01-DEC-99 1DJ3
TITLE STRUCTURES OF ADENYLOSUCCINATE SYNTHETASE FROM TRITICUM AESTIVUM AND
TITLE 2 ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLOSUCCINATE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 6.3.4.4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;
SOURCE 3 ORGANISM_COMMON: BREAD WHEAT;
SOURCE 4 ORGANISM_TAXID: 4565;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOSOL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET16B
KEYWDS GDP, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.PRADE,S.W.COWAN-JACOB,P.CHEMLA,S.POTTER,E.WARD,R.FONNE-PFISTER
REVDAT 4 07-FEB-24 1DJ3 1 REMARK SEQADV
REVDAT 3 04-OCT-17 1DJ3 1 REMARK
REVDAT 2 24-FEB-09 1DJ3 1 VERSN
REVDAT 1 24-MAR-00 1DJ3 0
JRNL AUTH L.PRADE,S.W.COWAN-JACOB,P.CHEMLA,S.POTTER,E.WARD,
JRNL AUTH 2 R.FONNE-PFISTER
JRNL TITL STRUCTURES OF ADENYLOSUCCINATE SYNTHETASE FROM TRITICUM
JRNL TITL 2 AESTIVUM AND ARABIDOPSIS THALIANA.
JRNL REF J.MOL.BIOL. V. 296 569 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10669609
JRNL DOI 10.1006/JMBI.1999.3473
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 18544
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) : 0.240
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 905
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6580
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.70
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 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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.139
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 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: NCS RESTRAINTS WERE SET.
REMARK 4
REMARK 4 1DJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010122.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20426
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 33.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
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) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, LITHIUM SULFATE, CITRATE, PH
REMARK 280 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 45.97000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 75.72000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 75.72000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.98500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 75.72000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 75.72000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 68.95500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 75.72000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.72000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.98500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 75.72000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.72000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.95500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 45.97000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 ALA A 4
REMARK 465 VAL A 5
REMARK 465 GLU A 6
REMARK 465 ALA A 7
REMARK 465 ASP A 8
REMARK 465 PRO A 9
REMARK 465 ALA A 10
REMARK 465 SER B 1
REMARK 465 ALA B 2
REMARK 465 LEU B 3
REMARK 465 ALA B 4
REMARK 465 VAL B 5
REMARK 465 GLU B 6
REMARK 465 ALA B 7
REMARK 465 ASP B 8
REMARK 465 PRO B 9
REMARK 465 ALA B 10
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 GLN A 129 CG CD OE1 NE2
REMARK 470 GLN B 129 CG CD OE1 NE2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA A 140
REMARK 475 ASN A 141
REMARK 475 SER A 142
REMARK 475 PHE A 143
REMARK 475 ILE A 144
REMARK 475 GLY A 145
REMARK 475 THR A 146
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 PHE A 143 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 PHE B 143 N - CA - C ANGL. DEV. = 17.7 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 GLN A 27 -128.52 -118.52
REMARK 500 ALA A 56 -133.31 -70.42
REMARK 500 ASN A 62 -160.68 -79.79
REMARK 500 HIS A 71 -64.96 -126.13
REMARK 500 ASN A 107 30.92 -94.45
REMARK 500 LEU A 139 -176.09 -65.13
REMARK 500 ALA A 140 -4.98 -51.49
REMARK 500 ASN A 141 76.02 84.02
REMARK 500 ILE A 144 105.76 26.93
REMARK 500 THR A 146 38.44 -77.96
REMARK 500 LYS A 148 29.78 -77.72
REMARK 500 ARG A 189 -70.89 -73.02
REMARK 500 TYR A 195 88.09 56.87
REMARK 500 ASP A 220 90.38 -65.81
REMARK 500 GLN A 241 -158.49 -131.56
REMARK 500 SER A 400 6.61 -64.51
REMARK 500 GLN B 27 -128.57 -118.89
REMARK 500 ALA B 56 -133.15 -70.84
REMARK 500 ASN B 62 -160.29 -79.26
REMARK 500 HIS B 71 -65.39 -126.50
REMARK 500 ASN B 107 30.61 -94.90
REMARK 500 LEU B 139 -176.00 -65.17
REMARK 500 ALA B 140 -4.37 -51.61
REMARK 500 ASN B 141 75.58 83.08
REMARK 500 ILE B 144 105.47 27.93
REMARK 500 THR B 146 38.52 -77.73
REMARK 500 LYS B 148 29.74 -78.22
REMARK 500 ARG B 189 -70.97 -72.92
REMARK 500 TYR B 195 88.48 56.89
REMARK 500 ASP B 220 90.13 -65.91
REMARK 500 GLN B 241 -158.49 -131.91
REMARK 500 SER B 400 6.91 -65.21
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 GDP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DJ2 RELATED DB: PDB
DBREF 1DJ3 A 1 442 UNP O24396 PURA_WHEAT 35 476
DBREF 1DJ3 B 1 442 UNP O24396 PURA_WHEAT 35 476
SEQADV 1DJ3 ASN A 19 UNP O24396 GLN 53 CONFLICT
SEQADV 1DJ3 LYS A 209 UNP O24396 ARG 243 CONFLICT
SEQADV 1DJ3 ASN B 19 UNP O24396 GLN 53 CONFLICT
SEQADV 1DJ3 LYS B 209 UNP O24396 ARG 243 CONFLICT
SEQRES 1 A 442 SER ALA LEU ALA VAL GLU ALA ASP PRO ALA ALA ASP ARG
SEQRES 2 A 442 VAL SER SER LEU SER ASN VAL SER GLY VAL LEU GLY SER
SEQRES 3 A 442 GLN TRP GLY ASP GLU GLY LYS GLY LYS LEU VAL ASP VAL
SEQRES 4 A 442 LEU ALA PRO ARG PHE ASP ILE VAL ALA ARG CYS GLN GLY
SEQRES 5 A 442 GLY ALA ASN ALA GLY HIS THR ILE TYR ASN SER GLU GLY
SEQRES 6 A 442 LYS LYS PHE ALA LEU HIS LEU VAL PRO SER GLY ILE LEU
SEQRES 7 A 442 HIS GLU GLY THR LEU CYS VAL VAL GLY ASN GLY ALA VAL
SEQRES 8 A 442 ILE HIS VAL PRO GLY PHE PHE GLY GLU ILE ASP GLY LEU
SEQRES 9 A 442 GLN SER ASN GLY VAL SER CYS ASP GLY ARG ILE LEU VAL
SEQRES 10 A 442 SER ASP ARG ALA HIS LEU LEU PHE ASP LEU HIS GLN THR
SEQRES 11 A 442 VAL ASP GLY LEU ARG GLU ALA GLU LEU ALA ASN SER PHE
SEQRES 12 A 442 ILE GLY THR THR LYS ARG GLY ILE GLY PRO CYS TYR SER
SEQRES 13 A 442 SER LYS VAL THR ARG ASN GLY LEU ARG VAL CYS ASP LEU
SEQRES 14 A 442 ARG HIS MET ASP THR PHE GLY ASP LYS LEU ASP VAL LEU
SEQRES 15 A 442 PHE GLU ASP ALA ALA ALA ARG PHE GLU GLY PHE LYS TYR
SEQRES 16 A 442 SER LYS GLY MET LEU LYS GLU GLU VAL GLU ARG TYR LYS
SEQRES 17 A 442 LYS PHE ALA GLU ARG LEU GLU PRO PHE ILE ALA ASP THR
SEQRES 18 A 442 VAL HIS VAL LEU ASN GLU SER ILE ARG GLN LYS LYS LYS
SEQRES 19 A 442 ILE LEU VAL GLU GLY GLY GLN ALA THR MET LEU ASP ILE
SEQRES 20 A 442 ASP PHE GLY THR TYR PRO PHE VAL THR SER SER SER PRO
SEQRES 21 A 442 SER ALA GLY GLY ILE CYS THR GLY LEU GLY ILE ALA PRO
SEQRES 22 A 442 ARG VAL ILE GLY ASP LEU ILE GLY VAL VAL LYS ALA TYR
SEQRES 23 A 442 THR THR ARG VAL GLY SER GLY PRO PHE PRO THR GLU LEU
SEQRES 24 A 442 LEU GLY GLU GLU GLY ASP VAL LEU ARG LYS ALA GLY MET
SEQRES 25 A 442 GLU PHE GLY THR THR THR GLY ARG PRO ARG ARG CYS GLY
SEQRES 26 A 442 TRP LEU ASP ILE VAL ALA LEU LYS TYR CYS CYS ASP ILE
SEQRES 27 A 442 ASN GLY PHE SER SER LEU ASN LEU THR LYS LEU ASP VAL
SEQRES 28 A 442 LEU SER GLY LEU PRO GLU ILE LYS LEU GLY VAL SER TYR
SEQRES 29 A 442 ASN GLN MET ASP GLY GLU LYS LEU GLN SER PHE PRO GLY
SEQRES 30 A 442 ASP LEU ASP THR LEU GLU GLN VAL GLN VAL ASN TYR GLU
SEQRES 31 A 442 VAL LEU PRO GLY TRP ASP SER ASP ILE SER SER VAL ARG
SEQRES 32 A 442 SER TYR SER GLU LEU PRO GLN ALA ALA ARG ARG TYR VAL
SEQRES 33 A 442 GLU ARG ILE GLU GLU LEU ALA GLY VAL PRO VAL HIS TYR
SEQRES 34 A 442 ILE GLY VAL GLY PRO GLY ARG ASP ALA LEU ILE TYR LYS
SEQRES 1 B 442 SER ALA LEU ALA VAL GLU ALA ASP PRO ALA ALA ASP ARG
SEQRES 2 B 442 VAL SER SER LEU SER ASN VAL SER GLY VAL LEU GLY SER
SEQRES 3 B 442 GLN TRP GLY ASP GLU GLY LYS GLY LYS LEU VAL ASP VAL
SEQRES 4 B 442 LEU ALA PRO ARG PHE ASP ILE VAL ALA ARG CYS GLN GLY
SEQRES 5 B 442 GLY ALA ASN ALA GLY HIS THR ILE TYR ASN SER GLU GLY
SEQRES 6 B 442 LYS LYS PHE ALA LEU HIS LEU VAL PRO SER GLY ILE LEU
SEQRES 7 B 442 HIS GLU GLY THR LEU CYS VAL VAL GLY ASN GLY ALA VAL
SEQRES 8 B 442 ILE HIS VAL PRO GLY PHE PHE GLY GLU ILE ASP GLY LEU
SEQRES 9 B 442 GLN SER ASN GLY VAL SER CYS ASP GLY ARG ILE LEU VAL
SEQRES 10 B 442 SER ASP ARG ALA HIS LEU LEU PHE ASP LEU HIS GLN THR
SEQRES 11 B 442 VAL ASP GLY LEU ARG GLU ALA GLU LEU ALA ASN SER PHE
SEQRES 12 B 442 ILE GLY THR THR LYS ARG GLY ILE GLY PRO CYS TYR SER
SEQRES 13 B 442 SER LYS VAL THR ARG ASN GLY LEU ARG VAL CYS ASP LEU
SEQRES 14 B 442 ARG HIS MET ASP THR PHE GLY ASP LYS LEU ASP VAL LEU
SEQRES 15 B 442 PHE GLU ASP ALA ALA ALA ARG PHE GLU GLY PHE LYS TYR
SEQRES 16 B 442 SER LYS GLY MET LEU LYS GLU GLU VAL GLU ARG TYR LYS
SEQRES 17 B 442 LYS PHE ALA GLU ARG LEU GLU PRO PHE ILE ALA ASP THR
SEQRES 18 B 442 VAL HIS VAL LEU ASN GLU SER ILE ARG GLN LYS LYS LYS
SEQRES 19 B 442 ILE LEU VAL GLU GLY GLY GLN ALA THR MET LEU ASP ILE
SEQRES 20 B 442 ASP PHE GLY THR TYR PRO PHE VAL THR SER SER SER PRO
SEQRES 21 B 442 SER ALA GLY GLY ILE CYS THR GLY LEU GLY ILE ALA PRO
SEQRES 22 B 442 ARG VAL ILE GLY ASP LEU ILE GLY VAL VAL LYS ALA TYR
SEQRES 23 B 442 THR THR ARG VAL GLY SER GLY PRO PHE PRO THR GLU LEU
SEQRES 24 B 442 LEU GLY GLU GLU GLY ASP VAL LEU ARG LYS ALA GLY MET
SEQRES 25 B 442 GLU PHE GLY THR THR THR GLY ARG PRO ARG ARG CYS GLY
SEQRES 26 B 442 TRP LEU ASP ILE VAL ALA LEU LYS TYR CYS CYS ASP ILE
SEQRES 27 B 442 ASN GLY PHE SER SER LEU ASN LEU THR LYS LEU ASP VAL
SEQRES 28 B 442 LEU SER GLY LEU PRO GLU ILE LYS LEU GLY VAL SER TYR
SEQRES 29 B 442 ASN GLN MET ASP GLY GLU LYS LEU GLN SER PHE PRO GLY
SEQRES 30 B 442 ASP LEU ASP THR LEU GLU GLN VAL GLN VAL ASN TYR GLU
SEQRES 31 B 442 VAL LEU PRO GLY TRP ASP SER ASP ILE SER SER VAL ARG
SEQRES 32 B 442 SER TYR SER GLU LEU PRO GLN ALA ALA ARG ARG TYR VAL
SEQRES 33 B 442 GLU ARG ILE GLU GLU LEU ALA GLY VAL PRO VAL HIS TYR
SEQRES 34 B 442 ILE GLY VAL GLY PRO GLY ARG ASP ALA LEU ILE TYR LYS
HET GDP A 500 28
HET GDP B 600 28
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
HELIX 1 1 ASP A 12 SER A 16 5 5
HELIX 2 2 GLY A 32 ALA A 41 1 10
HELIX 3 3 PRO A 42 PHE A 44 5 3
HELIX 4 4 PRO A 74 HIS A 79 5 6
HELIX 5 5 HIS A 93 SER A 106 1 14
HELIX 6 6 PHE A 125 LEU A 139 1 15
HELIX 7 7 GLY A 150 THR A 160 1 11
HELIX 8 8 VAL A 166 ARG A 170 5 5
HELIX 9 9 HIS A 171 PHE A 190 1 20
HELIX 10 10 SER A 196 GLU A 215 1 20
HELIX 11 11 ASP A 220 GLN A 231 1 12
HELIX 12 12 MET A 244 ASP A 246 5 3
HELIX 13 13 ALA A 262 GLY A 270 1 9
HELIX 14 14 ALA A 272 ILE A 276 5 5
HELIX 15 15 GLY A 301 MET A 312 1 12
HELIX 16 16 ILE A 329 GLY A 340 1 12
HELIX 17 17 LYS A 348 SER A 353 5 6
HELIX 18 18 ASP A 378 GLU A 383 1 6
HELIX 19 19 PRO A 409 GLY A 424 1 16
HELIX 20 20 ASP B 12 SER B 16 5 5
HELIX 21 21 GLY B 32 ALA B 41 1 10
HELIX 22 22 PRO B 42 PHE B 44 5 3
HELIX 23 23 PRO B 74 HIS B 79 5 6
HELIX 24 24 HIS B 93 SER B 106 1 14
HELIX 25 25 PHE B 125 LEU B 139 1 15
HELIX 26 26 GLY B 150 THR B 160 1 11
HELIX 27 27 VAL B 166 ARG B 170 5 5
HELIX 28 28 HIS B 171 PHE B 190 1 20
HELIX 29 29 SER B 196 GLU B 215 1 20
HELIX 30 30 ASP B 220 GLN B 231 1 12
HELIX 31 31 MET B 244 ASP B 246 5 3
HELIX 32 32 ALA B 262 GLY B 270 1 9
HELIX 33 33 ALA B 272 ILE B 276 5 5
HELIX 34 34 GLY B 301 MET B 312 1 12
HELIX 35 35 ILE B 329 GLY B 340 1 12
HELIX 36 36 LYS B 348 SER B 353 5 6
HELIX 37 37 ASP B 378 GLU B 383 1 6
HELIX 38 38 PRO B 409 GLY B 424 1 16
SHEET 1 A10 ILE A 218 ALA A 219 0
SHEET 2 A10 ILE A 115 SER A 118 1 O VAL A 117 N ALA A 219
SHEET 3 A10 LEU A 83 VAL A 86 1 O CYS A 84 N LEU A 116
SHEET 4 A10 ILE A 46 ARG A 49 1 O VAL A 47 N VAL A 85
SHEET 5 A10 ILE A 235 ALA A 242 1 N LEU A 236 O ILE A 46
SHEET 6 A10 VAL A 20 GLY A 25 1 O SER A 21 N VAL A 237
SHEET 7 A10 LEU A 279 LYS A 284 1 O ILE A 280 N LEU A 24
SHEET 8 A10 SER A 343 THR A 347 1 O SER A 343 N GLY A 281
SHEET 9 A10 TYR A 429 GLY A 431 1 O TYR A 429 N LEU A 346
SHEET 10 A10 LEU A 439 TYR A 441 -1 N ILE A 440 O ILE A 430
SHEET 1 B 2 HIS A 58 TYR A 61 0
SHEET 2 B 2 LYS A 67 LEU A 70 -1 O PHE A 68 N ILE A 60
SHEET 1 C 2 VAL A 91 ILE A 92 0
SHEET 2 C 2 HIS A 122 LEU A 123 1 O HIS A 122 N ILE A 92
SHEET 1 D 3 TYR A 286 ARG A 289 0
SHEET 2 D 3 ARG A 323 ASP A 328 -1 N ARG A 323 O ARG A 289
SHEET 3 D 3 LEU A 360 GLY A 361 1 N GLY A 361 O LEU A 327
SHEET 1 E 2 GLU A 357 ILE A 358 0
SHEET 2 E 2 LEU A 392 PRO A 393 -1 O LEU A 392 N ILE A 358
SHEET 1 F 2 SER A 363 ASN A 365 0
SHEET 2 F 2 GLN A 386 ASN A 388 -1 N GLN A 386 O ASN A 365
SHEET 1 G10 ILE B 218 ALA B 219 0
SHEET 2 G10 ILE B 115 SER B 118 1 O VAL B 117 N ALA B 219
SHEET 3 G10 LEU B 83 VAL B 86 1 O CYS B 84 N LEU B 116
SHEET 4 G10 ILE B 46 ARG B 49 1 O VAL B 47 N VAL B 85
SHEET 5 G10 ILE B 235 ALA B 242 1 N LEU B 236 O ILE B 46
SHEET 6 G10 VAL B 20 GLY B 25 1 O SER B 21 N VAL B 237
SHEET 7 G10 LEU B 279 LYS B 284 1 O ILE B 280 N LEU B 24
SHEET 8 G10 SER B 343 THR B 347 1 O SER B 343 N GLY B 281
SHEET 9 G10 VAL B 427 GLY B 431 1 N HIS B 428 O LEU B 344
SHEET 10 G10 LEU B 439 TYR B 441 -1 N ILE B 440 O ILE B 430
SHEET 1 H 2 HIS B 58 TYR B 61 0
SHEET 2 H 2 LYS B 67 LEU B 70 -1 O PHE B 68 N ILE B 60
SHEET 1 I 2 VAL B 91 ILE B 92 0
SHEET 2 I 2 HIS B 122 LEU B 123 1 O HIS B 122 N ILE B 92
SHEET 1 J 3 TYR B 286 ARG B 289 0
SHEET 2 J 3 ARG B 323 ASP B 328 -1 N ARG B 323 O ARG B 289
SHEET 3 J 3 LEU B 360 GLY B 361 1 N GLY B 361 O LEU B 327
SHEET 1 K 2 GLU B 357 ILE B 358 0
SHEET 2 K 2 LEU B 392 PRO B 393 -1 O LEU B 392 N ILE B 358
SHEET 1 L 2 SER B 363 ASN B 365 0
SHEET 2 L 2 GLN B 386 ASN B 388 -1 N GLN B 386 O ASN B 365
CISPEP 1 TYR A 252 PRO A 253 0 -0.02
CISPEP 2 TYR B 252 PRO B 253 0 -0.01
SITE 1 AC1 15 ASP A 30 GLU A 31 GLY A 32 LYS A 33
SITE 2 AC1 15 GLY A 34 LYS A 35 GLY A 57 HIS A 58
SITE 3 AC1 15 THR A 59 LYS A 348 ASP A 350 GLY A 431
SITE 4 AC1 15 VAL A 432 GLY A 433 PRO A 434
SITE 1 AC2 15 ASP B 30 GLU B 31 GLY B 32 LYS B 33
SITE 2 AC2 15 GLY B 34 LYS B 35 GLY B 57 HIS B 58
SITE 3 AC2 15 THR B 59 LYS B 348 ASP B 350 GLY B 431
SITE 4 AC2 15 VAL B 432 GLY B 433 PRO B 434
CRYST1 151.440 151.440 91.940 90.00 90.00 90.00 P 41 21 2 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 0.006603 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006603 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010877 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
