HEADER SIGNALING PROTEIN 28-OCT-00 1G4U
TITLE CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE
TITLE 2 AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE SPTP;
COMPND 3 CHAIN: S;
COMPND 4 FRAGMENT: SPTP RESIDUES 161-543;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;
COMPND 8 CHAIN: R;
COMPND 9 FRAGMENT: RAC1 RESIDUES 1-184;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 GENE: SPTP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-3;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: RAC1;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-3
KEYWDS VIRULENCE FACTOR, GAP, TYROSINE PHOSPHATASE, 4-HELIX BUNDLE,
KEYWDS 2 GTPASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.STEBBINS,J.E.GALAN
REVDAT 2 24-FEB-09 1G4U 1 VERSN
REVDAT 1 24-JAN-01 1G4U 0
JRNL AUTH C.E.STEBBINS,J.E.GALAN
JRNL TITL MODULATION OF HOST SIGNALING BY A BACTERIAL MIMIC:
JRNL TITL 2 STRUCTURE OF THE SALMONELLA EFFECTOR SPTP BOUND TO
JRNL TITL 3 RAC1.
JRNL REF MOL.CELL V. 6 1449 2000
JRNL REFN ISSN 1097-2765
JRNL PMID 11163217
JRNL DOI 10.1016/S1097-2765(00)00141-6
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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 : 26361
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 7% CNS
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2009
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) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 51
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 : 4188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 334
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.13
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.23
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.40
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 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 1G4U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-00.
REMARK 100 THE RCSB ID CODE IS RCSB012234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 5.7
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 RU200HB
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27264
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.42700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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 (%): 53.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18 %PEG 400, 0.1M MES, 15MM SODIUM
REMARK 280 FLOURIDE, 0.1MM ALUMINUM CHLORIDE, 2MM DTT, 2MM MAGNESIUM
REMARK 280 CHLORIDE, PH 5.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 323K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, R
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 ASN S 161
REMARK 465 ASP S 162
REMARK 465 VAL S 163
REMARK 465 GLY S 164
REMARK 465 ALA S 165
REMARK 465 GLU S 166
REMARK 465 SER S 461
REMARK 465 ASN S 462
REMARK 465 GLN S 463
REMARK 465 ASN S 464
REMARK 465 GLY S 465
REMARK 465 ALA S 466
REMARK 465 PRO S 467
REMARK 465 GLY S 468
REMARK 465 ARG S 469
REMARK 465 SER S 470
REMARK 465 SER S 471
REMARK 465 SER S 472
REMARK 465 ASP S 473
REMARK 465 THR S 540
REMARK 465 THR S 541
REMARK 465 ALA S 542
REMARK 465 SER S 543
REMARK 465 PRO R 181
REMARK 465 VAL R 182
REMARK 465 LYS R 183
REMARK 465 LYS R 184
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH S 545 O HOH S 640 2.10
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 ALA S 292 -122.11 -103.16
REMARK 500 ALA S 294 45.69 -90.77
REMARK 500 LEU S 305 40.32 38.27
REMARK 500 ALA S 344 170.41 178.49
REMARK 500 ARG S 391 -91.30 -105.06
REMARK 500 ALA S 409 -112.12 -22.72
REMARK 500 SER S 410 -75.93 -128.94
REMARK 500 CYS S 481 -115.00 -106.23
REMARK 500 PRO S 501 -16.59 -48.53
REMARK 500 ARG S 516 -68.83 -137.11
REMARK 500 ALA R 13 8.20 81.79
REMARK 500 PHE R 37 149.86 -174.61
REMARK 500 LYS R 96 -59.39 -139.86
REMARK 500 PRO R 106 -76.01 -28.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH S 577 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH R1108 DISTANCE = 5.61 ANGSTROMS
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 R1001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR R 17 OG1
REMARK 620 2 HOH R1073 O 80.2
REMARK 620 3 GDP R1000 O2B 79.5 83.9
REMARK 620 4 HOH R1072 O 86.0 162.3 82.8
REMARK 620 5 THR R 35 OG1 73.1 91.2 152.7 95.3
REMARK 620 6 AF3 R1002 F1 172.3 103.8 94.2 88.7 113.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 R1002 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH R1071 O
REMARK 620 2 GDP R1000 O3B 138.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP R 1000
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 R 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G4W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE
REMARK 900 AND GTPASE ACTIVATING PROTEIN SPTP
DBREF 1G4U S 161 543 UNP P74873 SPTP_SALTY 161 543
DBREF 1G4U R 1 184 UNP P63000 RAC1_HUMAN 1 184
SEQADV 1G4U SER R 78 UNP P63000 PHE 78 ENGINEERED
SEQRES 1 S 383 ASN ASP VAL GLY ALA GLU SER LYS GLN PRO LEU LEU ASP
SEQRES 2 S 383 ILE ALA LEU LYS GLY LEU LYS ARG THR LEU PRO GLN LEU
SEQRES 3 S 383 GLU GLN MET ASP GLY ASN SER LEU ARG GLU ASN PHE GLN
SEQRES 4 S 383 GLU MET ALA SER GLY ASN GLY PRO LEU ARG SER LEU MET
SEQRES 5 S 383 THR ASN LEU GLN ASN LEU ASN LYS ILE PRO GLU ALA LYS
SEQRES 6 S 383 GLN LEU ASN ASP TYR VAL THR THR LEU THR ASN ILE GLN
SEQRES 7 S 383 VAL GLY VAL ALA ARG PHE SER GLN TRP GLY THR CYS GLY
SEQRES 8 S 383 GLY GLU VAL GLU ARG TRP VAL ASP LYS ALA SER THR HIS
SEQRES 9 S 383 GLU LEU THR GLN ALA VAL LYS LYS ILE HIS VAL ILE ALA
SEQRES 10 S 383 LYS GLU LEU LYS ASN VAL THR ALA GLU LEU GLU LYS ILE
SEQRES 11 S 383 GLU ALA GLY ALA PRO MET PRO GLN THR MET SER GLY PRO
SEQRES 12 S 383 THR LEU GLY LEU ALA ARG PHE ALA VAL SER SER ILE PRO
SEQRES 13 S 383 ILE ASN GLN GLN THR GLN VAL LYS LEU SER ASP GLY MET
SEQRES 14 S 383 PRO VAL PRO VAL ASN THR LEU THR PHE ASP GLY LYS PRO
SEQRES 15 S 383 VAL ALA LEU ALA GLY SER TYR PRO LYS ASN THR PRO ASP
SEQRES 16 S 383 ALA LEU GLU ALA HIS MET LYS MET LEU LEU GLU LYS GLU
SEQRES 17 S 383 CYS SER CYS LEU VAL VAL LEU THR SER GLU ASP GLN MET
SEQRES 18 S 383 GLN ALA LYS GLN LEU PRO PRO TYR PHE ARG GLY SER TYR
SEQRES 19 S 383 THR PHE GLY GLU VAL HIS THR ASN SER GLN LYS VAL SER
SEQRES 20 S 383 SER ALA SER GLN GLY GLU ALA ILE ASP GLN TYR ASN MET
SEQRES 21 S 383 GLN LEU SER CYS GLY GLU LYS ARG TYR THR ILE PRO VAL
SEQRES 22 S 383 LEU HIS VAL LYS ASN TRP PRO ASP HIS GLN PRO LEU PRO
SEQRES 23 S 383 SER THR ASP GLN LEU GLU TYR LEU ALA ASP ARG VAL LYS
SEQRES 24 S 383 ASN SER ASN GLN ASN GLY ALA PRO GLY ARG SER SER SER
SEQRES 25 S 383 ASP LYS HIS LEU PRO MET ILE HIS CYS LEU GLY GLY VAL
SEQRES 26 S 383 GLY ARG THR GLY THR MET ALA ALA ALA LEU VAL LEU LYS
SEQRES 27 S 383 ASP ASN PRO HIS SER ASN LEU GLU GLN VAL ARG ALA ASP
SEQRES 28 S 383 PHE ARG ASP SER ARG ASN ASN ARG MET LEU GLU ASP ALA
SEQRES 29 S 383 SER GLN PHE VAL GLN LEU LYS ALA MET GLN ALA GLN LEU
SEQRES 30 S 383 LEU MET THR THR ALA SER
SEQRES 1 R 184 MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 R 184 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 R 184 ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN
SEQRES 4 R 184 TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN
SEQRES 5 R 184 LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 R 184 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL SER
SEQRES 7 R 184 LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU
SEQRES 8 R 184 ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS
SEQRES 9 R 184 CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU
SEQRES 10 R 184 ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS
SEQRES 11 R 184 GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU
SEQRES 12 R 184 ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU
SEQRES 13 R 184 CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE
SEQRES 14 R 184 ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL
SEQRES 15 R 184 LYS LYS
HET MG R1001 1
HET GDP R1000 28
HET AF3 R1002 4
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM AF3 ALUMINUM FLUORIDE
FORMUL 3 MG MG 2+
FORMUL 4 GDP C10 H15 N5 O11 P2
FORMUL 5 AF3 AL F3
FORMUL 6 HOH *334(H2 O)
HELIX 1 1 SER S 167 GLN S 188 1 22
HELIX 2 2 ASP S 190 GLU S 196 1 7
HELIX 3 3 ASN S 197 ALA S 202 1 6
HELIX 4 4 GLY S 206 ASN S 217 1 12
HELIX 5 5 LEU S 218 GLU S 223 5 6
HELIX 6 6 ALA S 224 ASN S 236 1 13
HELIX 7 7 PHE S 244 THR S 249 5 6
HELIX 8 8 GLY S 252 ALA S 261 1 10
HELIX 9 9 SER S 262 LEU S 280 1 19
HELIX 10 10 LEU S 280 ALA S 292 1 13
HELIX 11 11 THR S 353 GLU S 368 1 16
HELIX 12 12 SER S 377 LYS S 384 1 8
HELIX 13 13 SER S 447 ASN S 460 1 14
HELIX 14 14 GLY S 486 ASN S 500 1 15
HELIX 15 15 ASN S 504 ASP S 514 1 11
HELIX 16 16 ASP S 523 MET S 539 1 17
HELIX 17 17 GLY R 15 ASN R 26 1 12
HELIX 18 18 GLN R 61 ASP R 65 5 5
HELIX 19 19 LEU R 67 TYR R 72 5 6
HELIX 20 20 SER R 86 LYS R 96 1 11
HELIX 21 21 LYS R 96 CYS R 105 1 10
HELIX 22 22 LYS R 116 ARG R 120 5 5
HELIX 23 23 ASP R 122 LYS R 132 1 11
HELIX 24 24 THR R 138 GLY R 150 1 13
HELIX 25 25 GLY R 164 LEU R 177 1 14
SHEET 1 A 9 GLN S 322 LYS S 324 0
SHEET 2 A 9 PRO S 330 PHE S 338 -1 N VAL S 331 O VAL S 323
SHEET 3 A 9 LYS S 341 GLY S 347 -1 O LYS S 341 N PHE S 338
SHEET 4 A 9 PRO S 477 HIS S 480 1 O PRO S 477 N LEU S 345
SHEET 5 A 9 CYS S 371 VAL S 374 1 O CYS S 371 N MET S 478
SHEET 6 A 9 LYS S 427 VAL S 436 1 O PRO S 432 N LEU S 372
SHEET 7 A 9 ILE S 415 CYS S 424 -1 O ASP S 416 N HIS S 435
SHEET 8 A 9 VAL S 399 LYS S 405 -1 N HIS S 400 O SER S 423
SHEET 9 A 9 SER S 393 PHE S 396 -1 O TYR S 394 N THR S 401
SHEET 1 B 6 ASP R 38 VAL R 46 0
SHEET 2 B 6 LYS R 49 ASP R 57 -1 O LYS R 49 N VAL R 46
SHEET 3 B 6 GLN R 2 GLY R 10 1 O GLN R 2 N ASN R 52
SHEET 4 B 6 VAL R 77 SER R 83 1 O VAL R 77 N VAL R 7
SHEET 5 B 6 ILE R 110 THR R 115 1 O ILE R 111 N ILE R 80
SHEET 6 B 6 LYS R 153 GLU R 156 1 O LYS R 153 N LEU R 112
LINK MG MG R1001 OG1 THR R 17 1555 1555 2.43
LINK MG MG R1001 O HOH R1073 1555 1555 2.53
LINK MG MG R1001 O2B GDP R1000 1555 1555 2.36
LINK MG MG R1001 O HOH R1072 1555 1555 2.23
LINK MG MG R1001 OG1 THR R 35 1555 1555 2.46
LINK MG MG R1001 F1 AF3 R1002 1555 1555 2.43
LINK AL AF3 R1002 O HOH R1071 1555 1555 2.96
LINK AL AF3 R1002 O3B GDP R1000 1555 1555 2.79
SITE 1 AC1 6 THR R 17 THR R 35 GDP R1000 AF3 R1002
SITE 2 AC1 6 HOH R1072 HOH R1073
SITE 1 AC2 22 ALA R 13 VAL R 14 GLY R 15 LYS R 16
SITE 2 AC2 22 THR R 17 CYS R 18 LYS R 116 ASP R 118
SITE 3 AC2 22 SER R 158 ALA R 159 LEU R 160 MG R1001
SITE 4 AC2 22 AF3 R1002 HOH R1004 HOH R1010 HOH R1042
SITE 5 AC2 22 HOH R1072 HOH R1073 ARG S 209 THR S 249
SITE 6 AC2 22 CYS S 250 HOH S 680
SITE 1 AC3 10 GLY R 12 ALA R 13 LYS R 16 THR R 35
SITE 2 AC3 10 GLY R 60 GLN R 61 GDP R1000 MG R1001
SITE 3 AC3 10 HOH R1071 ARG S 209
CRYST1 56.722 58.260 60.324 70.03 69.51 65.03 P 1 1
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 0.017630 -0.008210 -0.004843 0.00000
SCALE2 0.000000 0.018934 -0.004437 0.00000
SCALE3 0.000000 0.000000 0.018176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
