HEADER TRANSLATION 03-FEB-06 2FX3
TITLE CRYSTAL STRUCTURE DETERMINATION OF E. COLI ELONGATION
TITLE 2 FACTOR, TU USING A TWINNED DATA SET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TU;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EF-TU
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 OTHER_DETAILS: GENE: TUFA
KEYWDS EF-TU, MEROHEDRAL TWINNING, TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.E.HEFFRON,R.MOELLER,F.JURNAK
REVDAT 2 24-FEB-09 2FX3 1 VERSN
REVDAT 1 28-MAR-06 2FX3 0
JRNL AUTH S.E.HEFFRON,R.MOELLER,F.JURNAK
JRNL TITL SOLVING THE STRUCTURE OF ESCHERICHIA COLI
JRNL TITL 2 ELONGATION FACTOR TU USING A TWINNED DATA SET.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 62 433 2006
JRNL REFN ISSN 0907-4449
JRNL PMID 16552145
JRNL DOI 10.1107/S0907444906004021
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.23
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) (%) : 87.1
REMARK 3 NUMBER OF REFLECTIONS : 6083
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : USED CNS TASK FILE MAKE_
REMARK 3 CV_TWIN.INP TO SELECT CROSS
REMARK 3 -VALIDATION SET SUCH THAT
REMARK 3 PAIRS OF TWIN-RELATED
REMARK 3 REFLECTIONS WERE DESIGNATED
REMARK 3 TO BE IN THE SAME SET,
REMARK 3 EITHER THE WORKING SET OR
REMARK 3 THE TEST SET.
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.400
REMARK 3 FREE R VALUE TEST SET COUNT : 586
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 : 2981
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.81900
REMARK 3 B22 (A**2) : 8.81900
REMARK 3 B33 (A**2) : -17.63900
REMARK 3 B12 (A**2) : 2.01100
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.73
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.69
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.18
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : 73.77
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : MYTOPPAR:GDP_CNS4.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED CNS SPECIALIZED TASK FILES FOR
REMARK 3 REFINEMENT WITH HEMIHEDRALLY TWINNED DATA. TWIN OPERATOR WAS
REMARK 3 (-H,-K,L), AND TWIN FRACTION WAS 0.294. R-FACTORS REPORTED ARE
REMARK 3 THE TWINNED R-FACTORS FROM CNS. (R-FACTORS AFTER DETWINNING: R
REMARK 3 -WORK=0.2867, R-FREE=0.3267)
REMARK 4
REMARK 4 2FX3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-06.
REMARK 100 THE RCSB ID CODE IS RCSB036414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6312
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 60.232
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.17400
REMARK 200 R SYM (I) : 0.17400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : 0.48000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1D8T, CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.45 MM EF-TU IN 50 MM TRIS, PH
REMARK 280 7.8, 10 MM GDP, 10 MM MAGNESIUM CHLORIDE, 0.5% PEG 3350, 5.5
REMARK 280 MM AMMONIUM ACETATE, 2.7 MM AMMONIUM CITRATE, 1.34 MM CHEMDIV
REMARK 280 COMPOUND 1013-0135, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.48000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 112.96000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 112.96000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.48000
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: MONOMERIC
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 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 LYS A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 PHE A 5
REMARK 465 GLU A 6
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 OG1 THR A 320 O THR A 38 3454 2.16
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 THR A 8 -33.67 114.19
REMARK 500 LYS A 9 107.79 -59.50
REMARK 500 PRO A 10 136.67 -39.43
REMARK 500 VAL A 14 -165.89 -129.37
REMARK 500 ALA A 29 -75.00 -45.77
REMARK 500 ALA A 30 -35.05 -33.66
REMARK 500 THR A 33 -74.77 -53.11
REMARK 500 GLN A 48 -19.86 -46.24
REMARK 500 GLU A 54 -159.10 -89.14
REMARK 500 ARG A 58 -0.74 56.05
REMARK 500 THR A 71 -167.71 -102.03
REMARK 500 PRO A 72 -74.39 -68.25
REMARK 500 ALA A 95 -33.34 -38.44
REMARK 500 PRO A 113 -74.87 -44.22
REMARK 500 LYS A 136 17.92 54.38
REMARK 500 GLU A 143 -74.44 -37.12
REMARK 500 VAL A 153 -82.66 -74.12
REMARK 500 ARG A 154 -27.93 -33.73
REMARK 500 PRO A 163 68.92 -65.77
REMARK 500 ALA A 182 -39.02 -37.85
REMARK 500 PRO A 202 173.63 -57.73
REMARK 500 LYS A 208 164.26 -45.57
REMARK 500 LEU A 212 114.11 -162.52
REMARK 500 SER A 221 -90.16 30.98
REMARK 500 ARG A 223 61.07 -161.58
REMARK 500 ILE A 247 -88.65 75.59
REMARK 500 SER A 253 -167.97 -164.09
REMARK 500 CYS A 255 98.94 -67.31
REMARK 500 PHE A 261 66.55 66.86
REMARK 500 ARG A 262 -1.79 49.69
REMARK 500 GLU A 267 139.48 -177.04
REMARK 500 ARG A 288 158.33 -48.85
REMARK 500 PRO A 295 101.83 -52.31
REMARK 500 ILE A 298 143.33 -171.85
REMARK 500 THR A 302 -24.81 -141.17
REMARK 500 LEU A 311 -177.91 -62.13
REMARK 500 ARG A 318 152.13 -43.90
REMARK 500 LYS A 324 173.63 -46.83
REMARK 500 ARG A 333 -57.91 60.32
REMARK 500 PRO A 344 154.56 -46.64
REMARK 500 LEU A 392 -77.53 -114.89
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 998 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 25 OG1
REMARK 620 2 GDP A 999 O2B 75.6
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 A 998
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 999
DBREF 2FX3 A 1 393 UNP Q83JC4 EFTU_SHIFL 1 393
SEQRES 1 A 393 SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN
SEQRES 2 A 393 VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR
SEQRES 3 A 393 LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR
SEQRES 4 A 393 GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA
SEQRES 5 A 393 PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER
SEQRES 6 A 393 HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS
SEQRES 7 A 393 VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET
SEQRES 8 A 393 ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL
SEQRES 9 A 393 VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU
SEQRES 10 A 393 HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE
SEQRES 11 A 393 ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU
SEQRES 12 A 393 GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU
SEQRES 13 A 393 LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE
SEQRES 14 A 393 VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA
SEQRES 15 A 393 GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU
SEQRES 16 A 393 ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS
SEQRES 17 A 393 PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER
SEQRES 18 A 393 GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY
SEQRES 19 A 393 ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE
SEQRES 20 A 393 LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET
SEQRES 21 A 393 PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN
SEQRES 22 A 393 VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE
SEQRES 23 A 393 GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS
SEQRES 24 A 393 PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER
SEQRES 25 A 393 LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY
SEQRES 26 A 393 TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR
SEQRES 27 A 393 GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET
SEQRES 28 A 393 PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS
SEQRES 29 A 393 PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG
SEQRES 30 A 393 GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS
SEQRES 31 A 393 VAL LEU GLY
HET MG A 998 1
HET GDP A 999 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 GDP C10 H15 N5 O11 P2
FORMUL 4 HOH *4(H2 O)
HELIX 1 1 GLY A 23 GLY A 40 1 18
HELIX 2 2 ALA A 45 ASN A 51 1 7
HELIX 3 3 GLY A 83 GLY A 94 1 12
HELIX 4 4 MET A 112 GLY A 126 1 15
HELIX 5 5 LYS A 136 VAL A 140 5 5
HELIX 6 6 ASP A 142 TYR A 160 1 19
HELIX 7 7 PRO A 163 THR A 167 5 5
HELIX 8 8 SER A 173 GLY A 180 1 8
HELIX 9 9 ASP A 181 ILE A 199 1 19
HELIX 10 10 LYS A 282 ILE A 286 5 5
SHEET 1 A 6 SER A 65 ASP A 70 0
SHEET 2 A 6 HIS A 75 ASP A 80 -1 O HIS A 78 N VAL A 67
SHEET 3 A 6 HIS A 11 GLY A 18 1 N VAL A 12 O ALA A 77
SHEET 4 A 6 ALA A 101 ALA A 106 1 O ILE A 102 N GLY A 15
SHEET 5 A 6 ILE A 130 ASN A 135 1 O ASN A 135 N VAL A 105
SHEET 6 A 6 ILE A 169 ARG A 171 1 O VAL A 170 N VAL A 132
SHEET 1 B 2 LYS A 56 ALA A 57 0
SHEET 2 B 2 ILE A 60 THR A 61 -1 O ILE A 60 N ALA A 57
SHEET 1 C 7 LEU A 211 PRO A 213 0
SHEET 2 C 7 VAL A 291 ALA A 293 -1 O LEU A 292 N LEU A 212
SHEET 3 C 7 GLU A 241 VAL A 245 -1 N GLU A 243 O ALA A 293
SHEET 4 C 7 GLN A 251 MET A 260 -1 O GLN A 251 N ILE A 244
SHEET 5 C 7 ASN A 273 LEU A 278 -1 O LEU A 277 N THR A 256
SHEET 6 C 7 THR A 225 ARG A 230 -1 N VAL A 227 O VAL A 276
SHEET 7 C 7 ASP A 216 PHE A 218 -1 N PHE A 218 O VAL A 226
SHEET 1 D 5 LEU A 211 PRO A 213 0
SHEET 2 D 5 VAL A 291 ALA A 293 -1 O LEU A 292 N LEU A 212
SHEET 3 D 5 GLU A 241 VAL A 245 -1 N GLU A 243 O ALA A 293
SHEET 4 D 5 GLN A 251 MET A 260 -1 O GLN A 251 N ILE A 244
SHEET 5 D 5 LYS A 263 LEU A 265 -1 O LEU A 265 N VAL A 258
SHEET 1 E 2 ILE A 235 LYS A 237 0
SHEET 2 E 2 GLU A 267 ARG A 269 -1 O GLY A 268 N ILE A 236
SHEET 1 F 6 GLN A 329 TYR A 331 0
SHEET 2 F 6 ARG A 373 GLU A 378 -1 O ARG A 377 N GLN A 329
SHEET 3 F 6 ARG A 381 VAL A 391 -1 O VAL A 383 N ILE A 376
SHEET 4 F 6 LYS A 299 ILE A 310 -1 N GLU A 305 O LYS A 390
SHEET 5 F 6 ASN A 355 MET A 368 -1 O MET A 358 N SER A 306
SHEET 6 F 6 GLY A 339 GLU A 342 -1 N THR A 340 O THR A 361
SHEET 1 G 2 PHE A 322 PHE A 323 0
SHEET 2 G 2 MET A 349 VAL A 350 -1 O VAL A 350 N PHE A 322
LINK MG MG A 998 OG1 THR A 25 1555 1555 2.14
LINK MG MG A 998 O2B GDP A 999 1555 1555 2.46
SITE 1 AC1 4 THR A 25 ASP A 50 CYS A 81 GDP A 999
SITE 1 AC2 17 HIS A 19 VAL A 20 ASP A 21 HIS A 22
SITE 2 AC2 17 GLY A 23 LYS A 24 THR A 25 THR A 26
SITE 3 AC2 17 PHE A 46 ASN A 135 LYS A 136 ASP A 138
SITE 4 AC2 17 MET A 139 SER A 173 ALA A 174 LEU A 175
SITE 5 AC2 17 MG A 998
CRYST1 69.550 69.550 169.440 90.00 90.00 120.00 P 31 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 0.014378 0.008301 0.000000 0.00000
SCALE2 0.000000 0.016602 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005902 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
