HEADER LIGASE 26-MAR-99 1CG3
TITLE STRUCTURE OF THE MUTANT (R143L) OF ADENYLOSUCCINATE SYNTHETASE FROM E.
TITLE 2 COLI COMPLEXED WITH HADACIDIN, GDP, 6-PHOSPHORYL-IMP, AND MG2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ADENYLOSUCCINATE SYNTHETASE);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMPSASE;
COMPND 5 EC: 6.3.4.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: PUR A- STRAIN H1238;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS LIGASE, GTP-HYDROLYSING ENZYMES, PURINE 2 NUCLEOTIDE BIOSYNTHESIS, 6-
KEYWDS 2 PHOSPORYL- IMP
EXPDTA X-RAY DIFFRACTION
AUTHOR J.Y.CHOE,B.W.POLAND,H.FROMM,R.HONZATKO
REVDAT 6 09-AUG-23 1CG3 1 REMARK SEQADV LINK
REVDAT 5 14-MAR-18 1CG3 1 SEQADV
REVDAT 4 04-OCT-17 1CG3 1 REMARK
REVDAT 3 13-JUL-11 1CG3 1 VERSN
REVDAT 2 24-FEB-09 1CG3 1 VERSN
REVDAT 1 17-JUN-99 1CG3 0
JRNL AUTH J.Y.CHOE,B.W.POLAND,H.J.FROMM,R.B.HONZATKO
JRNL TITL MECHANISTIC IMPLICATIONS FROM CRYSTALLINE COMPLEXES OF
JRNL TITL 2 WILD-TYPE AND MUTANT ADENYLOSUCCINATE SYNTHETASES FROM
JRNL TITL 3 ESCHERICHIA COLI.
JRNL REF BIOCHEMISTRY V. 38 6953 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10346917
JRNL DOI 10.1021/BI990159S
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 67.7
REMARK 3 NUMBER OF REFLECTIONS : 17987
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1799
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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 : 3318
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.00
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.890
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARNAH1E.DNA
REMARK 3 PARAMETER FILE 3 : PARAM19.SOL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.PEP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.5
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 : SIEMENS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : X-GEN
REMARK 200 DATA SCALING SOFTWARE : X-GEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.09080
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
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: X-PLOR
REMARK 200 STARTING MODEL: 1GIM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 8000, 100MM NA-CACODYLATE(PH
REMARK 280 6.5)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.499650 -0.854150 0.000000 0.00000
REMARK 290 SMTRY2 2 0.878066 -0.500350 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.48523
REMARK 290 SMTRY1 3 -0.500350 0.854150 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.878066 -0.499650 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.74262
REMARK 290 SMTRY1 4 -0.499650 0.854549 0.000000 0.00000
REMARK 290 SMTRY2 4 0.878066 0.499650 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 -0.000798 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.74262
REMARK 290 SMTRY1 6 -0.500350 -0.853751 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.878066 0.500350 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.48523
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 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 -0.500350 -0.853751 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.878066 0.500350 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 105.48523
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS A 160 OD2 ASP A 363 6555 1.98
REMARK 500 O HOH A 537 O HOH A 555 6555 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 7 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 LEU A 74 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 GLU A 373 N - CA - C ANGL. DEV. = -16.9 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 10 -107.76 -116.99
REMARK 500 HIS A 53 -69.89 -124.22
REMARK 500 LYS A 124 44.63 -105.21
REMARK 500 LEU A 151 -7.18 -56.05
REMARK 500 GLN A 224 -157.93 57.03
REMARK 500 ALA A 245 -28.48 -39.16
REMARK 500 ALA A 268 -12.07 92.03
REMARK 500 PHE A 278 74.23 -157.99
REMARK 500 LYS A 331 19.82 56.30
REMARK 500 LEU A 360 -82.18 -101.95
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 435 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 GLY A 40 O 171.5
REMARK 620 3 GDP A 432 O2B 108.2 79.3
REMARK 620 4 GDP A 432 O2A 95.3 89.0 86.6
REMARK 620 5 HDA A 437 O 83.5 88.4 162.8 105.3
REMARK 620 6 IMO A 440 O1 85.7 91.2 83.8 170.2 84.5
REMARK 620 N 1 2 3 4 5
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 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDA A 437
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMO A 440
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 432
DBREF 1CG3 A 1 431 UNP P0A7D4 PURA_ECOLI 1 431
SEQADV 1CG3 LEU A 143 UNP P0A7D4 ARG 143 ENGINEERED MUTATION
SEQRES 1 A 431 GLY ASN ASN VAL VAL VAL LEU GLY THR GLN TRP GLY ASP
SEQRES 2 A 431 GLU GLY LYS GLY LYS ILE VAL ASP LEU LEU THR GLU ARG
SEQRES 3 A 431 ALA LYS TYR VAL VAL ARG TYR GLN GLY GLY HIS ASN ALA
SEQRES 4 A 431 GLY HIS THR LEU VAL ILE ASN GLY GLU LYS THR VAL LEU
SEQRES 5 A 431 HIS LEU ILE PRO SER GLY ILE LEU ARG GLU ASN VAL THR
SEQRES 6 A 431 SER ILE ILE GLY ASN GLY VAL VAL LEU SER PRO ALA ALA
SEQRES 7 A 431 LEU MET LYS GLU MET LYS GLU LEU GLU ASP ARG GLY ILE
SEQRES 8 A 431 PRO VAL ARG GLU ARG LEU LEU LEU SER GLU ALA CYS PRO
SEQRES 9 A 431 LEU ILE LEU ASP TYR HIS VAL ALA LEU ASP ASN ALA ARG
SEQRES 10 A 431 GLU LYS ALA ARG GLY ALA LYS ALA ILE GLY THR THR GLY
SEQRES 11 A 431 ARG GLY ILE GLY PRO ALA TYR GLU ASP LYS VAL ALA LEU
SEQRES 12 A 431 ARG GLY LEU ARG VAL GLY ASP LEU PHE ASP LYS GLU THR
SEQRES 13 A 431 PHE ALA GLU LYS LEU LYS GLU VAL MET GLU TYR HIS ASN
SEQRES 14 A 431 PHE GLN LEU VAL ASN TYR TYR LYS ALA GLU ALA VAL ASP
SEQRES 15 A 431 TYR GLN LYS VAL LEU ASP ASP THR MET ALA VAL ALA ASP
SEQRES 16 A 431 ILE LEU THR SER MET VAL VAL ASP VAL SER ASP LEU LEU
SEQRES 17 A 431 ASP GLN ALA ARG GLN ARG GLY ASP PHE VAL MET PHE GLU
SEQRES 18 A 431 GLY ALA GLN GLY THR LEU LEU ASP ILE ASP HIS GLY THR
SEQRES 19 A 431 TYR PRO TYR VAL THR SER SER ASN THR THR ALA GLY GLY
SEQRES 20 A 431 VAL ALA THR GLY SER GLY LEU GLY PRO ARG TYR VAL ASP
SEQRES 21 A 431 TYR VAL LEU GLY ILE LEU LYS ALA TYR SER THR ARG VAL
SEQRES 22 A 431 GLY ALA GLY PRO PHE PRO THR GLU LEU PHE ASP GLU THR
SEQRES 23 A 431 GLY GLU PHE LEU CYS LYS GLN GLY ASN GLU PHE GLY ALA
SEQRES 24 A 431 THR THR GLY ARG ARG ARG ARG THR GLY TRP LEU ASP THR
SEQRES 25 A 431 VAL ALA VAL ARG ARG ALA VAL GLN LEU ASN SER LEU SER
SEQRES 26 A 431 GLY PHE CYS LEU THR LYS LEU ASP VAL LEU ASP GLY LEU
SEQRES 27 A 431 LYS GLU VAL LYS LEU CYS VAL ALA TYR ARG MET PRO ASP
SEQRES 28 A 431 GLY ARG GLU VAL THR THR THR PRO LEU ALA ALA ASP ASP
SEQRES 29 A 431 TRP LYS GLY VAL GLU PRO ILE TYR GLU THR MET PRO GLY
SEQRES 30 A 431 TRP SER GLU SER THR PHE GLY VAL LYS ASP ARG SER GLY
SEQRES 31 A 431 LEU PRO GLN ALA ALA LEU ASN TYR ILE LYS ARG ILE GLU
SEQRES 32 A 431 GLU LEU THR GLY VAL PRO ILE ASP ILE ILE SER THR GLY
SEQRES 33 A 431 PRO ASP ARG THR GLU THR MET ILE LEU ARG ASP PRO PHE
SEQRES 34 A 431 ASP ALA
HET MG A 435 1
HET HDA A 437 8
HET IMO A 440 27
HET GDP A 432 28
HETNAM MG MAGNESIUM ION
HETNAM HDA HADACIDIN
HETNAM IMO 6-O-PHOSPHORYL INOSINE MONOPHOSPHATE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 HDA C3 H5 N O4
FORMUL 4 IMO C10 H14 N4 O11 P2
FORMUL 5 GDP C10 H15 N5 O11 P2
FORMUL 6 HOH *247(H2 O)
HELIX 1 1 LYS A 16 GLU A 25 1 10
HELIX 2 2 SER A 57 LEU A 60 5 4
HELIX 3 3 PRO A 76 GLU A 87 1 12
HELIX 4 4 VAL A 93 ARG A 96 1 4
HELIX 5 5 ASP A 108 ALA A 120 1 13
HELIX 6 6 GLY A 122 LYS A 124 5 3
HELIX 7 7 ILE A 133 VAL A 141 1 9
HELIX 8 8 GLY A 149 PHE A 152 5 4
HELIX 9 9 LYS A 154 ASN A 174 1 21
HELIX 10 10 TYR A 183 MET A 200 1 18
HELIX 11 11 VAL A 204 ARG A 214 1 11
HELIX 12 12 THR A 226 LEU A 228 5 3
HELIX 13 13 ALA A 245 SER A 252 5 8
HELIX 14 14 PRO A 256 TYR A 258 5 3
HELIX 15 15 GLU A 285 GLN A 293 1 9
HELIX 16 16 THR A 312 ASN A 322 1 11
HELIX 17 17 LEU A 332 LEU A 335 5 4
HELIX 18 18 ALA A 362 TRP A 365 5 4
HELIX 19 19 ARG A 388 GLY A 390 5 3
HELIX 20 20 GLN A 393 THR A 406 1 14
SHEET 1 A 9 THR A 422 ILE A 424 0
SHEET 2 A 9 ILE A 410 SER A 414 -1 N ILE A 413 O MET A 423
SHEET 3 A 9 GLY A 326 LEU A 329 1 N PHE A 327 O ASP A 411
SHEET 4 A 9 TYR A 261 LEU A 266 1 N GLY A 264 O GLY A 326
SHEET 5 A 9 ASN A 3 GLY A 8 1 N VAL A 5 O TYR A 261
SHEET 6 A 9 VAL A 218 GLU A 221 1 N VAL A 218 O VAL A 4
SHEET 7 A 9 TYR A 29 ARG A 32 1 N TYR A 29 O MET A 219
SHEET 8 A 9 THR A 65 ILE A 68 1 N THR A 65 O VAL A 30
SHEET 9 A 9 LEU A 97 LEU A 99 1 N LEU A 98 O SER A 66
SHEET 1 B 2 HIS A 41 ILE A 45 0
SHEET 2 B 2 GLU A 48 LEU A 52 -1 N LEU A 52 O HIS A 41
SHEET 1 C 2 SER A 270 ARG A 272 0
SHEET 2 C 2 ARG A 306 GLY A 308 -1 N GLY A 308 O SER A 270
SHEET 1 D 2 GLU A 340 ARG A 348 0
SHEET 2 D 2 GLU A 369 PRO A 376 -1 N MET A 375 O VAL A 341
LINK OD1 ASP A 13 MG MG A 435 1555 1555 2.16
LINK O GLY A 40 MG MG A 435 1555 1555 2.04
LINK O2B GDP A 432 MG MG A 435 1555 1555 2.10
LINK O2A GDP A 432 MG MG A 435 1555 1555 2.17
LINK MG MG A 435 O HDA A 437 1555 1555 2.11
LINK MG MG A 435 O1 IMO A 440 1555 1555 2.13
CISPEP 1 TYR A 235 PRO A 236 0 -3.58
SITE 1 AC1 5 ASP A 13 GLY A 40 GDP A 432 HDA A 437
SITE 2 AC1 5 IMO A 440
SITE 1 AC2 12 ASP A 13 ASN A 38 GLY A 40 GLY A 298
SITE 2 AC2 12 ALA A 299 THR A 300 THR A 301 ARG A 303
SITE 3 AC2 12 ARG A 305 GDP A 432 MG A 435 IMO A 440
SITE 1 AC3 29 TRP A 11 GLY A 12 ASP A 13 LYS A 16
SITE 2 AC3 29 ASN A 38 ALA A 39 GLY A 40 HIS A 41
SITE 3 AC3 29 GLY A 127 THR A 128 THR A 129 ILE A 133
SITE 4 AC3 29 ALA A 223 GLN A 224 VAL A 238 THR A 239
SITE 5 AC3 29 VAL A 273 GLY A 274 ARG A 303 GDP A 432
SITE 6 AC3 29 MG A 435 HDA A 437 HOH A 532 HOH A 585
SITE 7 AC3 29 HOH A 634 HOH A 659 HOH A 674 HOH A 676
SITE 8 AC3 29 HOH A 701
SITE 1 AC4 23 ASP A 13 GLU A 14 GLY A 15 LYS A 16
SITE 2 AC4 23 GLY A 17 GLY A 40 HIS A 41 THR A 42
SITE 3 AC4 23 ALA A 299 ARG A 305 LYS A 331 ASP A 333
SITE 4 AC4 23 SER A 414 THR A 415 GLY A 416 PRO A 417
SITE 5 AC4 23 MG A 435 HDA A 437 IMO A 440 HOH A 503
SITE 6 AC4 23 HOH A 716 HOH A 720 HOH A 738
CRYST1 80.940 80.940 158.180 90.00 90.00 120.00 P 32 2 1 6
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 0.012530 0.007130 0.000000 0.00000
SCALE2 0.000000 0.014270 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END