HEADER LIGASE 09-AUG-02 1MF0
TITLE STRUCTURE OF THE RECOMBINANT MOUSE-MUSCLE ADENYLOSUCCINATE SYNTHETASE
TITLE 2 COMPLEXED WITH AMP, GDP, HPO4(2-), AND MG(2+)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLOSUCCINATE SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ADSS, AMPSASE;
COMPND 5 EC: 6.3.4.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ADSS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS PURINE BIOSYNTHESIS, GTP-BINDING, MULTIGENE FAMILY, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.V.IANCU,T.BORZA,H.J.FROMM,R.B.HONZATKO
REVDAT 5 13-MAR-24 1MF0 1 REMARK LINK
REVDAT 4 11-OCT-17 1MF0 1 REMARK
REVDAT 3 13-JUL-11 1MF0 1 VERSN
REVDAT 2 24-FEB-09 1MF0 1 VERSN
REVDAT 1 30-OCT-02 1MF0 0
JRNL AUTH C.V.IANCU,T.BORZA,H.J.FROMM,R.B.HONZATKO
JRNL TITL FEEDBACK INHIBITION AND PRODUCT COMPLEXES OF RECOMBINANT
JRNL TITL 2 MOUSE MUSCLE ADENYLOSUCCINATE SYNTHETASE.
JRNL REF J.BIOL.CHEM. V. 277 40536 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12186864
JRNL DOI 10.1074/JBC.M204952200
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
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 : 17562
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) : 0.219
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1738
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 273
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3353
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 107
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 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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
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 1MF0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016862.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18179
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, PH 7, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 99.19500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.30000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 148.79250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.30000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.30000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.59750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.30000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.30000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 148.79250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.30000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.30000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.59750
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 99.19500
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: THE BIOLOGICAL UNIT IS A DIMER. THE OTHER MONOMER IS
REMARK 300 GENERATED BY:2-Y, 2-X, 1/2-Z.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
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 BIOMT1 2 0.000000 -1.000000 0.000000 141.20000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 141.20000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 99.19500
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 SER A 2
REMARK 465 GLY A 3
REMARK 465 THR A 4
REMARK 465 ARG A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 ASN A 8
REMARK 465 ASP A 9
REMARK 465 ARG A 10
REMARK 465 PRO A 11
REMARK 465 PRO A 12
REMARK 465 GLY A 13
REMARK 465 THR A 14
REMARK 465 GLY A 15
REMARK 465 GLY A 16
REMARK 465 VAL A 17
REMARK 465 LYS A 18
REMARK 465 ARG A 19
REMARK 465 GLY A 20
REMARK 465 ARG A 21
REMARK 465 LEU A 22
REMARK 465 GLN A 23
REMARK 465 GLN A 24
REMARK 465 GLU A 25
REMARK 465 ALA A 26
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 40 -116.87 -117.83
REMARK 500 ALA A 57 140.64 -24.52
REMARK 500 HIS A 83 -40.65 -138.29
REMARK 500 LYS A 118 32.38 -67.44
REMARK 500 LYS A 119 -0.95 -146.17
REMARK 500 GLN A 155 -78.86 -107.56
REMARK 500 SER A 187 -158.43 -66.56
REMARK 500 PRO A 208 -3.19 -58.65
REMARK 500 PRO A 247 136.19 -36.63
REMARK 500 ASN A 256 -137.88 52.78
REMARK 500 ASN A 316 -162.02 -173.58
REMARK 500 VAL A 331 23.21 -65.09
REMARK 500 THR A 332 -59.08 -163.96
REMARK 500 PRO A 424 -80.13 -30.09
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 A1453 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 43 OD1
REMARK 620 2 GLY A 70 O 158.8
REMARK 620 3 PO4 A1451 O1 88.1 105.2
REMARK 620 4 GDP A1452 O2A 80.2 79.4 144.1
REMARK 620 5 GDP A1452 O2B 85.5 80.5 81.0 64.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 1454
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 1452
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MEZ RELATED DB: PDB
REMARK 900 1MEZ CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH
REMARK 900 GDP, 2SA, MG AND SO4
REMARK 900 RELATED ID: 1MF1 RELATED DB: PDB
REMARK 900 1MF1 CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH
REMARK 900 AMP AND ACT
DBREF 1MF0 A 1 457 UNP P28650 PURA1_MOUSE 1 457
SEQRES 1 A 457 MET SER GLY THR ARG ALA SER ASN ASP ARG PRO PRO GLY
SEQRES 2 A 457 THR GLY GLY VAL LYS ARG GLY ARG LEU GLN GLN GLU ALA
SEQRES 3 A 457 ALA ALA THR GLY SER ARG VAL THR VAL VAL LEU GLY ALA
SEQRES 4 A 457 GLN TRP GLY ASP GLU GLY LYS GLY LYS VAL VAL ASP LEU
SEQRES 5 A 457 LEU ALA THR ASP ALA ASP ILE VAL SER ARG CYS GLN GLY
SEQRES 6 A 457 GLY ASN ASN ALA GLY HIS THR VAL VAL VAL ASP GLY LYS
SEQRES 7 A 457 GLU TYR ASP PHE HIS LEU LEU PRO SER GLY ILE ILE ASN
SEQRES 8 A 457 THR LYS ALA VAL SER PHE ILE GLY ASN GLY VAL VAL ILE
SEQRES 9 A 457 HIS LEU PRO GLY LEU PHE GLU GLU ALA GLU LYS ASN GLU
SEQRES 10 A 457 LYS LYS GLY LEU LYS ASP TRP GLU LYS ARG LEU ILE ILE
SEQRES 11 A 457 SER ASP ARG ALA HIS LEU VAL PHE ASP PHE HIS GLN ALA
SEQRES 12 A 457 VAL ASP GLY LEU GLN GLU VAL GLN ARG GLN ALA GLN GLU
SEQRES 13 A 457 GLY LYS ASN ILE GLY THR THR LYS LYS GLY ILE GLY PRO
SEQRES 14 A 457 THR TYR SER SER LYS ALA ALA ARG THR GLY LEU ARG ILE
SEQRES 15 A 457 CYS ASP LEU LEU SER ASP PHE ASP GLU PHE SER ALA ARG
SEQRES 16 A 457 PHE LYS ASN LEU ALA HIS GLN HIS GLN SER MET PHE PRO
SEQRES 17 A 457 THR LEU GLU ILE ASP VAL GLU GLY GLN LEU LYS ARG LEU
SEQRES 18 A 457 LYS GLY PHE ALA GLU ARG ILE ARG PRO MET VAL ARG ASP
SEQRES 19 A 457 GLY VAL TYR PHE MET TYR GLU ALA LEU HIS GLY PRO PRO
SEQRES 20 A 457 LYS LYS VAL LEU VAL GLU GLY ALA ASN ALA ALA LEU LEU
SEQRES 21 A 457 ASP ILE ASP PHE GLY THR TYR PRO PHE VAL THR SER SER
SEQRES 22 A 457 ASN CYS THR VAL GLY GLY VAL CYS THR GLY LEU GLY ILE
SEQRES 23 A 457 PRO PRO GLN ASN ILE GLY ASP VAL TYR GLY VAL VAL LYS
SEQRES 24 A 457 ALA TYR THR THR ARG VAL GLY ILE GLY ALA PHE PRO THR
SEQRES 25 A 457 GLU GLN ILE ASN GLU ILE GLY ASP LEU LEU GLN ASN ARG
SEQRES 26 A 457 GLY HIS GLU TRP GLY VAL THR THR GLY ARG LYS ARG ARG
SEQRES 27 A 457 CYS GLY TRP LEU ASP LEU MET ILE LEU ARG TYR ALA HIS
SEQRES 28 A 457 MET VAL ASN GLY PHE THR ALA LEU ALA LEU THR LYS LEU
SEQRES 29 A 457 ASP ILE LEU ASP VAL LEU SER GLU ILE LYS VAL GLY ILE
SEQRES 30 A 457 SER TYR LYS LEU ASN GLY LYS ARG ILE PRO TYR PHE PRO
SEQRES 31 A 457 ALA ASN GLN GLU ILE LEU GLN LYS VAL GLU VAL GLU TYR
SEQRES 32 A 457 GLU THR LEU PRO GLY TRP LYS ALA ASP THR THR GLY ALA
SEQRES 33 A 457 ARG LYS TRP GLU ASP LEU PRO PRO GLN ALA GLN SER TYR
SEQRES 34 A 457 VAL ARG PHE VAL GLU ASN HIS MET GLY VAL ALA VAL LYS
SEQRES 35 A 457 TRP VAL GLY VAL GLY LYS SER ARG GLU SER MET ILE GLN
SEQRES 36 A 457 LEU PHE
HET MG A1453 1
HET PO4 A1451 5
HET AMP A1454 23
HET GDP A1452 28
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 PO4 O4 P 3-
FORMUL 4 AMP C10 H14 N5 O7 P
FORMUL 5 GDP C10 H15 N5 O11 P2
FORMUL 6 HOH *107(H2 O)
HELIX 1 1 GLY A 45 THR A 55 1 11
HELIX 2 2 PRO A 86 ASN A 91 5 6
HELIX 3 3 HIS A 105 LYS A 118 1 14
HELIX 4 4 ASP A 123 LYS A 126 5 4
HELIX 5 5 PHE A 138 GLY A 157 1 20
HELIX 6 6 GLY A 166 ALA A 176 1 11
HELIX 7 7 ARG A 181 SER A 187 1 7
HELIX 8 8 ASP A 188 PHE A 207 1 20
HELIX 9 9 ASP A 213 ARG A 229 1 17
HELIX 10 10 ASP A 234 GLY A 245 1 12
HELIX 11 11 ALA A 257 ASP A 261 5 5
HELIX 12 12 VAL A 277 GLY A 285 1 9
HELIX 13 13 PRO A 287 GLN A 289 5 3
HELIX 14 14 ASN A 316 GLY A 326 1 11
HELIX 15 15 LEU A 344 GLY A 355 1 12
HELIX 16 16 LYS A 363 ASP A 368 5 6
HELIX 17 17 ASN A 392 GLN A 397 1 6
HELIX 18 18 PRO A 423 MET A 437 1 15
SHEET 1 A10 VAL A 232 ARG A 233 0
SHEET 2 A10 LEU A 128 SER A 131 1 N ILE A 130 O ARG A 233
SHEET 3 A10 VAL A 95 ILE A 98 1 N ILE A 98 O SER A 131
SHEET 4 A10 ILE A 59 ARG A 62 1 N VAL A 60 O PHE A 97
SHEET 5 A10 VAL A 250 GLU A 253 1 O GLU A 253 N SER A 61
SHEET 6 A10 VAL A 33 GLY A 38 1 N THR A 34 O VAL A 252
SHEET 7 A10 ILE A 291 LYS A 299 1 O ASP A 293 N VAL A 35
SHEET 8 A10 ALA A 358 THR A 362 1 O ALA A 360 N VAL A 298
SHEET 9 A10 VAL A 441 GLY A 445 1 O GLY A 445 N LEU A 361
SHEET 10 A10 MET A 453 GLN A 455 -1 O ILE A 454 N VAL A 444
SHEET 1 B 2 HIS A 71 VAL A 75 0
SHEET 2 B 2 LYS A 78 PHE A 82 -1 O TYR A 80 N VAL A 73
SHEET 1 C 2 VAL A 103 ILE A 104 0
SHEET 2 C 2 HIS A 135 LEU A 136 1 O HIS A 135 N ILE A 104
SHEET 1 D 2 THR A 302 ARG A 304 0
SHEET 2 D 2 ARG A 338 GLY A 340 -1 O GLY A 340 N THR A 302
SHEET 1 E 3 LEU A 342 ASP A 343 0
SHEET 2 E 3 GLU A 372 LYS A 380 1 O GLY A 376 N LEU A 342
SHEET 3 E 3 GLU A 400 PRO A 407 -1 O LEU A 406 N ILE A 373
LINK OD1 ASP A 43 MG MG A1453 1555 1555 1.92
LINK O GLY A 70 MG MG A1453 1555 1555 2.01
LINK O1 PO4 A1451 MG MG A1453 1555 1555 2.14
LINK O2A GDP A1452 MG MG A1453 1555 1555 2.15
LINK O2B GDP A1452 MG MG A1453 1555 1555 2.38
CISPEP 1 TYR A 267 PRO A 268 0 -0.26
SITE 1 AC1 4 ASP A 43 GLY A 70 PO4 A1451 GDP A1452
SITE 1 AC2 10 GLY A 42 ASP A 43 LYS A 46 ALA A 69
SITE 2 AC2 10 GLY A 70 HIS A 71 ASN A 256 GDP A1452
SITE 3 AC2 10 MG A1453 AMP A1454
SITE 1 AC3 16 ASP A 43 ASN A 68 ALA A 69 GLY A 70
SITE 2 AC3 16 THR A 162 THR A 163 ARG A 177 VAL A 270
SITE 3 AC3 16 THR A 271 ARG A 304 VAL A 305 GLY A 306
SITE 4 AC3 16 HOH A 520 HOH A 521 HOH A 579 PO4 A1451
SITE 1 AC4 20 ASP A 43 GLU A 44 GLY A 45 LYS A 46
SITE 2 AC4 20 GLY A 47 LYS A 48 GLY A 70 HIS A 71
SITE 3 AC4 20 THR A 72 LYS A 363 ASP A 365 ILE A 366
SITE 4 AC4 20 GLY A 445 VAL A 446 GLY A 447 LYS A 448
SITE 5 AC4 20 HOH A 503 HOH A 535 PO4 A1451 MG A1453
CRYST1 70.600 70.600 198.390 90.00 90.00 90.00 P 43 21 2 8
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 0.014164 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005041 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
