HEADER TRANSLATION 26-APR-01 1IJF
TITLE NUCLEOTIDE EXCHANGE MECHANISMS IN THE EEF1A-EEF1BA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR 1-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EEF1A;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ELONGATION FACTOR 1-BETA;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: CATALYTICAL C-TERMINAL FRAGMENT;
COMPND 9 SYNONYM: EEF1BA;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 4932;
SOURCE 9 GENE: TEF5;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: 834 DE3;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS PROTEIN COMPLEX, TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.R.ANDERSEN,L.VALENTE,L.PEDERSEN,T.G.KINZY,J.NYBORG
REVDAT 4 16-AUG-23 1IJF 1 REMARK LINK
REVDAT 3 24-FEB-09 1IJF 1 VERSN
REVDAT 2 06-JUN-01 1IJF 1 JRNL
REVDAT 1 09-MAY-01 1IJF 0
JRNL AUTH G.R.ANDERSEN,L.VALENTE,L.PEDERSEN,T.G.KINZY,J.NYBORG
JRNL TITL CRYSTAL STRUCTURES OF NUCLEOTIDE EXCHANGE INTERMEDIATES IN
JRNL TITL 2 THE EEF1A-EEF1BALPHA COMPLEX.
JRNL REF NAT.STRUCT.BIOL. V. 8 531 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11373622
JRNL DOI 10.1038/88598
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.R.ANDERSEN,L.PEDERSEN,L.VALENTE,I.I.CHATTERJEE,T.G.KINZY,
REMARK 1 AUTH 2 M.KJELDGAARD,J.NYBORG
REMARK 1 TITL STRUCTURAL BASIS FOR NUCLEOTIDE EXCHANGE AND COMPETITION
REMARK 1 TITL 2 WITH TRNA IN THE YEAST ELONGATION FACTOR COMPLEX
REMARK 1 TITL 3 EEF1A:EEF1BALPHA
REMARK 1 REF MOL.CELL V. 6 1261 2000
REMARK 1 REFN ISSN 1097-2765
REMARK 1 DOI 10.1016/S1097-2765(00)00122-2
REMARK 2
REMARK 2 RESOLUTION. 3.00 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 AND HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 133306.040
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 10866
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) : 0.250
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 573
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1457
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 87
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.042
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4091
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 14.06000
REMARK 3 B22 (A**2) : -1.98000
REMARK 3 B33 (A**2) : -12.08000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.44
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) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.56
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.010
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.360 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.020 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.020 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.960 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 10.00
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : 5GP_PAR500
REMARK 3 PARAMETER FILE 4 : MG135.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : 5GP_TOP
REMARK 3 TOPOLOGY FILE 4 : MG_XPLOR_TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10905
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 14.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.8000
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) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.17200
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1F60
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MME2K, TRIS, HEPES, KCL, DTT, PH 8.2,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 32.12350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.35650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.86400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.35650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.12350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.86400
REMARK 290 SMTRY3 4 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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 MET A 1
REMARK 465 THR A 442
REMARK 465 GLU A 443
REMARK 465 LYS A 444
REMARK 465 ALA A 445
REMARK 465 ALA A 446
REMARK 465 LYS A 447
REMARK 465 VAL A 448
REMARK 465 THR A 449
REMARK 465 LYS A 450
REMARK 465 ALA A 451
REMARK 465 ALA A 452
REMARK 465 GLN A 453
REMARK 465 LYS A 454
REMARK 465 ALA A 455
REMARK 465 ALA A 456
REMARK 465 LYS A 457
REMARK 465 LYS A 458
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 ALA A 279 CA - C - O ANGL. DEV. = -18.8 DEGREES
REMARK 500 PRO A 280 CA - N - CD ANGL. DEV. = -11.2 DEGREES
REMARK 500 PRO A 280 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO A 280 N - CD - CG ANGL. DEV. = 9.2 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 MET A 199 -64.42 -90.37
REMARK 500 PRO A 239 37.03 -74.15
REMARK 500 HIS A 293 -122.09 55.33
REMARK 500 ASN A 329 87.92 -166.53
REMARK 500 HIS A 362 -122.02 44.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 279 PRO A 280 56.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 279 22.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GDP A 507
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F60 RELATED DB: PDB
REMARK 900 1F60 IS YEAST ELONGATION FACTOR COMPLEX EEF1A: EEF1BA, NUCLEOTIDE
REMARK 900 FREE COMPLEX
REMARK 900 RELATED ID: 1G7C RELATED DB: PDB
REMARK 900 1G7C IS YEAST EEF1A: EEF1BA IN COMPLEX WITH GDPNP
REMARK 900 RELATED ID: 1IJE RELATED DB: PDB
REMARK 900 1IJE IS YEAST EEF1A: EEF1BA IN COMPLEX WITH GDP
DBREF 1IJF A 1 458 UNP P02994 EF1A_YEAST 1 458
DBREF 1IJF B 1117 1206 UNP P32471 EF1B_YEAST 117 206
SEQRES 1 A 458 MET GLY LYS GLU LYS SER HIS ILE ASN VAL VAL VAL ILE
SEQRES 2 A 458 GLY HIS VAL ASP SER GLY LYS SER THR THR THR GLY HIS
SEQRES 3 A 458 LEU ILE TYR LYS CYS GLY GLY ILE ASP LYS ARG THR ILE
SEQRES 4 A 458 GLU LYS PHE GLU LYS GLU ALA ALA GLU LEU GLY LYS GLY
SEQRES 5 A 458 SER PHE LYS TYR ALA TRP VAL LEU ASP LYS LEU LYS ALA
SEQRES 6 A 458 GLU ARG GLU ARG GLY ILE THR ILE ASP ILE ALA LEU TRP
SEQRES 7 A 458 LYS PHE GLU THR PRO LYS TYR GLN VAL THR VAL ILE ASP
SEQRES 8 A 458 ALA PRO GLY HIS ARG ASP PHE ILE LYS ASN MET ILE THR
SEQRES 9 A 458 GLY THR SER GLN ALA ASP CYS ALA ILE LEU ILE ILE ALA
SEQRES 10 A 458 GLY GLY VAL GLY GLU PHE GLU ALA GLY ILE SER LYS ASP
SEQRES 11 A 458 GLY GLN THR ARG GLU HIS ALA LEU LEU ALA PHE THR LEU
SEQRES 12 A 458 GLY VAL ARG GLN LEU ILE VAL ALA VAL ASN LYS MET ASP
SEQRES 13 A 458 SER VAL LYS TRP ASP GLU SER ARG PHE GLN GLU ILE VAL
SEQRES 14 A 458 LYS GLU THR SER ASN PHE ILE LYS LYS VAL GLY TYR ASN
SEQRES 15 A 458 PRO LYS THR VAL PRO PHE VAL PRO ILE SER GLY TRP ASN
SEQRES 16 A 458 GLY ASP ASN MET ILE GLU ALA THR THR ASN ALA PRO TRP
SEQRES 17 A 458 TYR LYS GLY TRP GLU LYS GLU THR LYS ALA GLY VAL VAL
SEQRES 18 A 458 LYS GLY LYS THR LEU LEU GLU ALA ILE ASP ALA ILE GLU
SEQRES 19 A 458 GLN PRO SER ARG PRO THR ASP LYS PRO LEU ARG LEU PRO
SEQRES 20 A 458 LEU GLN ASP VAL TYR LYS ILE GLY GLY ILE GLY THR VAL
SEQRES 21 A 458 PRO VAL GLY ARG VAL GLU THR GLY VAL ILE LYS PRO GLY
SEQRES 22 A 458 MET VAL VAL THR PHE ALA PRO ALA GLY VAL THR THR GLU
SEQRES 23 A 458 VAL LYS SER VAL GLU MET HIS HIS GLU GLN LEU GLU GLN
SEQRES 24 A 458 GLY VAL PRO GLY ASP ASN VAL GLY PHE ASN VAL LYS ASN
SEQRES 25 A 458 VAL SER VAL LYS GLU ILE ARG ARG GLY ASN VAL CYS GLY
SEQRES 26 A 458 ASP ALA LYS ASN ASP PRO PRO LYS GLY CYS ALA SER PHE
SEQRES 27 A 458 ASN ALA THR VAL ILE VAL LEU ASN HIS PRO GLY GLN ILE
SEQRES 28 A 458 SER ALA GLY TYR SER PRO VAL LEU ASP CYS HIS THR ALA
SEQRES 29 A 458 HIS ILE ALA CYS ARG PHE ASP GLU LEU LEU GLU LYS ASN
SEQRES 30 A 458 ASP ARG ARG SER GLY LYS LYS LEU GLU ASP HIS PRO LYS
SEQRES 31 A 458 PHE LEU LYS SER GLY ASP ALA ALA LEU VAL LYS PHE VAL
SEQRES 32 A 458 PRO SER LYS PRO MET CYS VAL GLU ALA PHE SER GLU TYR
SEQRES 33 A 458 PRO PRO LEU GLY ARG PHE ALA VAL ARG ASP MET ARG GLN
SEQRES 34 A 458 THR VAL ALA VAL GLY VAL ILE LYS SER VAL ASP LYS THR
SEQRES 35 A 458 GLU LYS ALA ALA LYS VAL THR LYS ALA ALA GLN LYS ALA
SEQRES 36 A 458 ALA LYS LYS
SEQRES 1 B 90 PRO ALA ALA LYS SER ILE VAL THR LEU ASP VAL LYS PRO
SEQRES 2 B 90 TRP ASP ASP GLU THR ASN LEU GLU GLU MET VAL ALA ASN
SEQRES 3 B 90 VAL LYS ALA ILE GLU MET GLU GLY LEU THR TRP GLY ALA
SEQRES 4 B 90 HIS GLN PHE ILE PRO ILE GLY PHE GLY ILE LYS LYS LEU
SEQRES 5 B 90 GLN ILE ASN CYS VAL VAL GLU ASP ASP LYS VAL SER LEU
SEQRES 6 B 90 ASP ASP LEU GLN GLN SER ILE GLU GLU ASP GLU ASP HIS
SEQRES 7 B 90 VAL GLN SER THR ASP ILE ALA ALA MET GLN LYS LEU
HET GDP A 507 24
HET MG B 508 1
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 3 GDP C10 H15 N5 O11 P2
FORMUL 4 MG MG 2+
HELIX 1 1 GLY A 19 GLY A 32 1 14
HELIX 2 2 ASP A 35 ALA A 46 1 12
HELIX 3 3 ALA A 47 GLY A 50 5 4
HELIX 4 4 LYS A 55 ARG A 69 1 15
HELIX 5 5 ASP A 97 GLY A 105 1 9
HELIX 6 6 GLY A 119 ILE A 127 1 9
HELIX 7 7 GLY A 131 LEU A 143 1 13
HELIX 8 8 LYS A 154 LYS A 159 5 6
HELIX 9 9 ASP A 161 GLY A 180 1 20
HELIX 10 10 ASN A 182 VAL A 186 5 5
HELIX 11 11 THR A 225 ALA A 232 1 8
HELIX 12 12 TYR A 416 LEU A 419 5 4
HELIX 13 13 ASN B 1135 ALA B 1145 1 11
HELIX 14 14 SER B 1180 GLU B 1189 1 10
SHEET 1 A 6 PHE A 188 PRO A 190 0
SHEET 2 A 6 GLN A 147 ASN A 153 1 O VAL A 150 N VAL A 189
SHEET 3 A 6 CYS A 111 ALA A 117 1 N ALA A 112 O GLN A 147
SHEET 4 A 6 SER A 6 ILE A 13 1 O ASN A 9 N CYS A 111
SHEET 5 A 6 TYR A 85 ASP A 91 1 N GLN A 86 O SER A 6
SHEET 6 A 6 TRP A 78 GLU A 81 -1 O TRP A 78 N VAL A 89
SHEET 1 B 2 TRP A 212 GLU A 215 0
SHEET 2 B 2 VAL A 220 GLY A 223 -1 N VAL A 221 O LYS A 214
SHEET 1 C 8 GLU A 295 GLN A 296 0
SHEET 2 C 8 VAL A 283 MET A 292 -1 N MET A 292 O GLU A 295
SHEET 3 C 8 VAL A 275 ALA A 279 -1 N VAL A 276 O THR A 285
SHEET 4 C 8 VAL A 323 ASP A 326 -1 O VAL A 323 N ALA A 279
SHEET 5 C 8 ARG A 245 ILE A 254 -1 O LEU A 246 N CYS A 324
SHEET 6 C 8 GLY A 258 ARG A 264 -1 N GLY A 258 O ILE A 254
SHEET 7 C 8 ASN A 305 VAL A 310 -1 N VAL A 306 O GLY A 263
SHEET 8 C 8 VAL A 283 MET A 292 -1 N LYS A 288 O ASN A 309
SHEET 1 D 8 LYS A 384 ASP A 387 0
SHEET 2 D 8 ALA A 364 ASN A 377 -1 O LYS A 376 N LEU A 385
SHEET 3 D 8 VAL A 358 CYS A 361 -1 N LEU A 359 O ILE A 366
SHEET 4 D 8 ARG A 421 ASP A 426 -1 O ALA A 423 N ASP A 360
SHEET 5 D 8 GLN A 429 ASP A 440 -1 O GLN A 429 N ASP A 426
SHEET 6 D 8 SER A 337 VAL A 344 -1 O SER A 337 N ASP A 440
SHEET 7 D 8 ALA A 397 PRO A 404 -1 O ALA A 398 N VAL A 342
SHEET 8 D 8 ALA A 364 ASN A 377 -1 N ARG A 369 O VAL A 403
SHEET 1 E 4 VAL B1195 LYS B1205 0
SHEET 2 E 4 LYS B1120 PRO B1129 -1 N ILE B1122 O GLN B1204
SHEET 3 E 4 ILE B1165 GLU B1175 -1 O LEU B1168 N VAL B1127
SHEET 4 E 4 LEU B1151 GLY B1162 -1 O THR B1152 N VAL B1173
LINK O2A GDP A 507 MG MG B 508 1555 1555 2.18
SITE 1 AC1 2 GDP A 507 LYS B1205
SITE 1 AC2 12 VAL A 16 GLY A 19 SER A 21 THR A 22
SITE 2 AC2 12 ASN A 153 LYS A 154 ASP A 156 SER A 192
SITE 3 AC2 12 GLY A 193 TRP A 194 MG B 508 LYS B1205
CRYST1 64.247 91.728 92.713 90.00 90.00 90.00 P 21 21 21 4
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 0.015565 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010902 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010786 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
