HEADER RIBOSOMAL PROTEIN 23-JUL-15 5A9X
TITLE STRUCTURE OF GDP BOUND BIPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BIPA;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: TRANSLATIONAL GTPASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA T1R;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS RIBOSOMAL PROTEIN, BIPA, RIBOSOME, TRANSLATIONAL GTPASE FACTORS
EXPDTA X-RAY DIFFRACTION
AUTHOR V.KUMAR,Y.CHEN,R.ERO,Z.LI,Y.-G.GAO
REVDAT 4 08-MAY-24 5A9X 1 REMARK
REVDAT 3 16-SEP-15 5A9X 1 JRNL
REVDAT 2 02-SEP-15 5A9X 1 JRNL
REVDAT 1 26-AUG-15 5A9X 0
JRNL AUTH V.KUMAR,Y.CHEN,R.ERO,T.AHMED,J.TAN,Z.LI,A.S.W.WONG,
JRNL AUTH 2 S.BHUSHAN,Y.GAO
JRNL TITL STRUCTURE OF BIPA IN GTP FORM BOUND TO THE RATCHETED
JRNL TITL 2 RIBOSOME.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 112 10944 2015
JRNL REFN ISSN 0027-8424
JRNL PMID 26283392
JRNL DOI 10.1073/PNAS.1513216112
REMARK 2
REMARK 2 RESOLUTION. 3.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 10584
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 + TEST SET) : 0.254
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.313
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1176
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 539
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.6950
REMARK 3 BIN FREE R VALUE SET COUNT : 60
REMARK 3 BIN FREE R VALUE : 0.7030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4138
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 240.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.783
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 1.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 89.909
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4224 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4055 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5745 ; 1.521 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9291 ; 1.066 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 550 ; 8.580 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 187 ;37.611 ;25.027
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 672 ;19.577 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;19.541 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 681 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4867 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 904 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2218 ;12.884 ;23.877
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2217 ;12.884 ;23.876
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2762 ;21.151 ;35.784
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2763 ;21.147 ;35.785
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2002 ;10.561 ;24.518
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1994 ;10.556 ;24.515
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2970 ;18.312 ;36.528
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4616 ;28.573 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4614 ;28.578 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5A9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1290064473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10596
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800
REMARK 200 RESOLUTION RANGE LOW (A) : 47.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 17.80
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG3350, 0.2 M SODIUM
REMARK 280 FLUORIDE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4
REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4
REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4
REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4
REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4
REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4
REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4
REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4
REMARK 290 25555 X+1/2,Y+1/2,Z+1/2
REMARK 290 26555 -X,-Y+1/2,Z
REMARK 290 27555 -X+1/2,Y,-Z
REMARK 290 28555 X,-Y,-Z+1/2
REMARK 290 29555 Z+1/2,X+1/2,Y+1/2
REMARK 290 30555 Z,-X,-Y+1/2
REMARK 290 31555 -Z,-X+1/2,Y
REMARK 290 32555 -Z+1/2,X,-Y
REMARK 290 33555 Y+1/2,Z+1/2,X+1/2
REMARK 290 34555 -Y+1/2,Z,-X
REMARK 290 35555 Y,-Z,-X+1/2
REMARK 290 36555 -Y,-Z+1/2,X
REMARK 290 37555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 38555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 39555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 40555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 41555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 42555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 43555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 44555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 45555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 46555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 47555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 48555 -Z+1/4,-Y+1/4,-X+1/4
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 120.97300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 120.97300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 120.97300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 120.97300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 120.97300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 120.97300
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 120.97300
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 120.97300
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 120.97300
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 120.97300
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 120.97300
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 120.97300
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 120.97300
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 181.45950
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 60.48650
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 181.45950
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 181.45950
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 60.48650
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 181.45950
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 60.48650
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 60.48650
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 60.48650
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 60.48650
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 181.45950
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 60.48650
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 181.45950
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 181.45950
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 60.48650
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 181.45950
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 181.45950
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 60.48650
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 60.48650
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 60.48650
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 60.48650
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 181.45950
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 181.45950
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 181.45950
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 120.97300
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 120.97300
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 120.97300
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 120.97300
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 120.97300
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 120.97300
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 120.97300
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 120.97300
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 120.97300
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 120.97300
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 120.97300
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 120.97300
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 120.97300
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 60.48650
REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 181.45950
REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 60.48650
REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 60.48650
REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 181.45950
REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 60.48650
REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 181.45950
REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 181.45950
REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 181.45950
REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 181.45950
REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 60.48650
REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 181.45950
REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 60.48650
REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 60.48650
REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 181.45950
REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 60.48650
REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 60.48650
REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 181.45950
REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 181.45950
REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 181.45950
REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 60.48650
REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 181.45950
REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 60.48650
REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 181.45950
REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 60.48650
REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 60.48650
REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 60.48650
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 THR A 31
REMARK 465 PHE A 32
REMARK 465 ASP A 33
REMARK 465 SER A 34
REMARK 465 ARG A 35
REMARK 465 ALA A 36
REMARK 465 GLU A 37
REMARK 465 THR A 38
REMARK 465 GLN A 39
REMARK 465 GLU A 40
REMARK 465 ARG A 41
REMARK 465 VAL A 42
REMARK 465 MET A 43
REMARK 465 ASP A 44
REMARK 465 SER A 45
REMARK 465 ASN A 46
REMARK 465 ASP A 47
REMARK 465 LEU A 48
REMARK 465 GLU A 49
REMARK 465 ILE A 63
REMARK 465 LYS A 64
REMARK 465 TRP A 65
REMARK 465 ASN A 66
REMARK 465 GLY A 170
REMARK 465 ILE A 171
REMARK 465 ALA A 172
REMARK 465 GLY A 278
REMARK 465 LEU A 279
REMARK 465 GLY A 280
REMARK 465 GLY A 540
REMARK 465 LYS A 541
REMARK 465 LYS A 542
REMARK 465 LEU A 543
REMARK 465 THR A 544
REMARK 465 ASN A 545
REMARK 465 MET A 546
REMARK 465 ARG A 547
REMARK 465 ALA A 548
REMARK 465 SER A 549
REMARK 465 GLY A 550
REMARK 465 THR A 551
REMARK 465 ASP A 552
REMARK 465 GLU A 553
REMARK 465 ALA A 554
REMARK 465 VAL A 555
REMARK 465 VAL A 556
REMARK 465 ALA A 603
REMARK 465 PRO A 604
REMARK 465 LYS A 605
REMARK 465 ASP A 606
REMARK 465 ASP A 607
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 24 CG CD CE NZ
REMARK 470 LYS A 59 CG CD CE NZ
REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 102 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 110 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 111 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 PHE A 160 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 161 CG CD
REMARK 470 LYS A 230 CG CD CE NZ
REMARK 470 HIS A 257 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 310 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 321 CG CD CE NZ
REMARK 470 GLU A 351 CG CD OE1 OE2
REMARK 470 LYS A 386 CG CD CE NZ
REMARK 470 PHE A 389 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 390 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 395 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 396 CG CD CE NZ
REMARK 470 LEU A 405 CD2
REMARK 470 GLU A 408 CG CD OE1 OE2
REMARK 470 GLU A 421 CG CD OE1 OE2
REMARK 470 LYS A 423 CG CD CE NZ
REMARK 470 LYS A 427 CG CD CE NZ
REMARK 470 ASN A 430 CG OD1 ND2
REMARK 470 ARG A 438 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 446 CG CD NE CZ NH1 NH2
REMARK 470 MET A 458 CG SD CE
REMARK 470 TYR A 466 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 473 CG OD1 OD2
REMARK 470 ASP A 474 CG OD1 OD2
REMARK 470 ARG A 476 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 499 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 509 CG CD CE NZ
REMARK 470 LEU A 512 CD1
REMARK 470 GLN A 522 CG CD OE1 NE2
REMARK 470 ILE A 523 CG1 CG2 CD1
REMARK 470 ILE A 524 CG1 CG2 CD1
REMARK 470 ARG A 562 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 588 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 589 CG CD CE NZ
REMARK 470 ARG A 590 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 594 CG CD OE1 OE2
REMARK 470 ASN A 595 CG OD1 ND2
REMARK 470 ARG A 598 CG CD NE CZ NH1 NH2
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 HIS A 16 O2B GDP A 1603 1.25
REMARK 500 CA GLY A 17 O3B GDP A 1603 1.42
REMARK 500 C GLY A 17 O3B GDP A 1603 1.81
REMARK 500 O GLU A 181 N MET A 183 1.99
REMARK 500 CG2 ILE A 240 OG1 THR A 287 2.07
REMARK 500 OE2 GLU A 177 N ALA A 180 2.10
REMARK 500 O ALA A 180 N ASP A 182 2.17
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 21 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 PRO A 161 N - CA - CB ANGL. DEV. = 7.8 DEGREES
REMARK 500 PRO A 477 C - N - CD ANGL. DEV. = 16.4 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 VAL A 14 -59.21 -11.54
REMARK 500 THR A 20 -102.39 58.85
REMARK 500 LEU A 21 -57.63 -121.58
REMARK 500 ASP A 23 -76.25 -74.99
REMARK 500 LEU A 26 82.26 -69.34
REMARK 500 SER A 29 130.42 71.46
REMARK 500 GLU A 51 -157.90 -166.32
REMARK 500 ILE A 56 82.37 45.20
REMARK 500 ALA A 58 179.74 -55.20
REMARK 500 ASP A 80 -84.30 -64.54
REMARK 500 ASP A 103 -78.31 -96.54
REMARK 500 PHE A 148 -24.48 -164.53
REMARK 500 ASP A 152 -160.46 44.34
REMARK 500 ALA A 153 -65.68 -175.22
REMARK 500 ASP A 155 -160.46 -61.69
REMARK 500 GLU A 156 88.14 44.32
REMARK 500 GLN A 157 -96.76 65.42
REMARK 500 PHE A 160 93.00 169.39
REMARK 500 PRO A 161 -169.39 60.51
REMARK 500 ILE A 162 33.70 77.64
REMARK 500 ALA A 167 -79.02 -97.33
REMARK 500 LEU A 168 87.25 -42.97
REMARK 500 ASP A 175 -159.82 46.56
REMARK 500 MET A 179 94.13 -167.14
REMARK 500 ALA A 180 -164.26 -69.63
REMARK 500 GLU A 181 72.31 -45.19
REMARK 500 ASP A 182 58.23 -45.11
REMARK 500 ASP A 202 -162.26 -100.70
REMARK 500 TYR A 217 14.67 -149.81
REMARK 500 ILE A 223 127.00 69.61
REMARK 500 ASP A 241 -44.15 104.45
REMARK 500 SER A 242 -135.08 -102.26
REMARK 500 GLU A 243 28.21 -157.46
REMARK 500 ALA A 249 -59.02 -122.36
REMARK 500 HIS A 257 3.20 -66.10
REMARK 500 ASP A 266 -88.30 -76.15
REMARK 500 ALA A 270 90.68 -69.57
REMARK 500 SER A 285 -33.72 73.14
REMARK 500 CYS A 289 -167.50 -128.00
REMARK 500 ASP A 290 -162.20 -62.65
REMARK 500 ASN A 293 79.28 43.69
REMARK 500 VAL A 294 -165.50 -167.51
REMARK 500 GLU A 295 130.59 74.72
REMARK 500 ALA A 296 -152.03 -134.71
REMARK 500 PRO A 298 -141.27 -99.13
REMARK 500 ALA A 299 86.33 77.10
REMARK 500 LEU A 300 -79.89 -60.14
REMARK 500 PRO A 317 39.20 -66.44
REMARK 500 PHE A 318 51.60 -146.26
REMARK 500 LYS A 321 -72.74 -76.13
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
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 THR A 20 LEU A 21 -143.31
REMARK 500 LEU A 25 LEU A 26 148.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 1603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A9V RELATED DB: PDB
REMARK 900 STRUCTURE OF APO BIPA
REMARK 900 RELATED ID: 5A9W RELATED DB: PDB
REMARK 900 STRUCTURE OF GDPCP BIPA
REMARK 900 RELATED ID: 5A9Y RELATED DB: PDB
REMARK 900 STRUCTURE OF PPGPP BIPA
REMARK 900 RELATED ID: 5A9Z RELATED DB: PDB
REMARK 900 COMPLEX OF THERMOUS THERMOPHILUS RIBOSOME BOUND TO BIPA -GDPCP
REMARK 900 RELATED ID: 5AA0 RELATED DB: PDB
REMARK 900 COMPLEX OF THERMOUS THERMOPHILUS RIBOSOME (A-AND P- SITE TRNA) TO
REMARK 900 BOUND BIPA-GDPCP
DBREF 5A9X A 1 607 UNP B7MHF0 B7MHF0_ECO45 1 607
SEQRES 1 A 607 MET ILE GLU LYS LEU ARG ASN ILE ALA ILE ILE ALA HIS
SEQRES 2 A 607 VAL ASP HIS GLY LYS THR THR LEU VAL ASP LYS LEU LEU
SEQRES 3 A 607 GLN GLN SER GLY THR PHE ASP SER ARG ALA GLU THR GLN
SEQRES 4 A 607 GLU ARG VAL MET ASP SER ASN ASP LEU GLU LYS GLU ARG
SEQRES 5 A 607 GLY ILE THR ILE LEU ALA LYS ASN THR ALA ILE LYS TRP
SEQRES 6 A 607 ASN ASP TYR ARG ILE ASN ILE VAL ASP THR PRO GLY HIS
SEQRES 7 A 607 ALA ASP PHE GLY GLY GLU VAL GLU ARG VAL MET SER MET
SEQRES 8 A 607 VAL ASP SER VAL LEU LEU VAL VAL ASP ALA PHE ASP GLY
SEQRES 9 A 607 PRO MET PRO GLN THR ARG PHE VAL THR LYS LYS ALA PHE
SEQRES 10 A 607 ALA TYR GLY LEU LYS PRO ILE VAL VAL ILE ASN LYS VAL
SEQRES 11 A 607 ASP ARG PRO GLY ALA ARG PRO ASP TRP VAL VAL ASP GLN
SEQRES 12 A 607 VAL PHE ASP LEU PHE VAL ASN LEU ASP ALA THR ASP GLU
SEQRES 13 A 607 GLN LEU ASP PHE PRO ILE VAL TYR ALA SER ALA LEU ASN
SEQRES 14 A 607 GLY ILE ALA GLY LEU ASP HIS GLU ASP MET ALA GLU ASP
SEQRES 15 A 607 MET THR PRO LEU TYR GLN ALA ILE VAL ASP HIS VAL PRO
SEQRES 16 A 607 ALA PRO ASP VAL ASP LEU ASP GLY PRO PHE GLN MET GLN
SEQRES 17 A 607 ILE SER GLN LEU ASP TYR ASN SER TYR VAL GLY VAL ILE
SEQRES 18 A 607 GLY ILE GLY ARG ILE LYS ARG GLY LYS VAL LYS PRO ASN
SEQRES 19 A 607 GLN GLN VAL THR ILE ILE ASP SER GLU GLY LYS THR ARG
SEQRES 20 A 607 ASN ALA LYS VAL GLY LYS VAL LEU GLY HIS LEU GLY LEU
SEQRES 21 A 607 GLU ARG ILE GLU THR ASP LEU ALA GLU ALA GLY ASP ILE
SEQRES 22 A 607 VAL ALA ILE THR GLY LEU GLY GLU LEU ASN ILE SER ASP
SEQRES 23 A 607 THR VAL CYS ASP THR GLN ASN VAL GLU ALA LEU PRO ALA
SEQRES 24 A 607 LEU SER VAL ASP GLU PRO THR VAL SER MET PHE PHE CYS
SEQRES 25 A 607 VAL ASN THR SER PRO PHE CYS GLY LYS GLU GLY LYS PHE
SEQRES 26 A 607 VAL THR SER ARG GLN ILE LEU ASP ARG LEU ASN LYS GLU
SEQRES 27 A 607 LEU VAL HIS ASN VAL ALA LEU ARG VAL GLU GLU THR GLU
SEQRES 28 A 607 ASP ALA ASP ALA PHE ARG VAL SER GLY ARG GLY GLU LEU
SEQRES 29 A 607 HIS LEU SER VAL LEU ILE GLU ASN MET ARG ARG GLU GLY
SEQRES 30 A 607 PHE GLU LEU ALA VAL SER ARG PRO LYS VAL ILE PHE ARG
SEQRES 31 A 607 GLU ILE ASP GLY ARG LYS GLN GLU PRO TYR GLU ASN VAL
SEQRES 32 A 607 THR LEU ASP VAL GLU GLU GLN HIS GLN GLY SER VAL MET
SEQRES 33 A 607 GLN ALA LEU GLY GLU ARG LYS GLY ASP LEU LYS ASN MET
SEQRES 34 A 607 ASN PRO ASP GLY LYS GLY ARG VAL ARG LEU ASP TYR VAL
SEQRES 35 A 607 ILE PRO SER ARG GLY LEU ILE GLY PHE ARG SER GLU PHE
SEQRES 36 A 607 MET THR MET THR SER GLY THR GLY LEU LEU TYR SER THR
SEQRES 37 A 607 PHE SER HIS TYR ASP ASP VAL ARG PRO GLY GLU VAL GLY
SEQRES 38 A 607 GLN ARG GLN ASN GLY VAL LEU ILE SER ASN GLY GLN GLY
SEQRES 39 A 607 LYS ALA VAL ALA PHE ALA LEU PHE GLY LEU GLN ASP ARG
SEQRES 40 A 607 GLY LYS LEU PHE LEU GLY HIS GLY ALA GLU VAL TYR GLU
SEQRES 41 A 607 GLY GLN ILE ILE GLY ILE HIS SER ARG SER ASN ASP LEU
SEQRES 42 A 607 THR VAL ASN CYS LEU THR GLY LYS LYS LEU THR ASN MET
SEQRES 43 A 607 ARG ALA SER GLY THR ASP GLU ALA VAL VAL LEU VAL PRO
SEQRES 44 A 607 PRO ILE ARG MET THR LEU GLU GLN ALA LEU GLU PHE ILE
SEQRES 45 A 607 ASP ASP ASP GLU LEU VAL GLU VAL THR PRO THR SER ILE
SEQRES 46 A 607 ARG ILE ARG LYS ARG HIS LEU THR GLU ASN ASP ARG ARG
SEQRES 47 A 607 ARG ALA ASN ARG ALA PRO LYS ASP ASP
HET GDP A1603 28
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 GDP C10 H15 N5 O11 P2
FORMUL 3 HOH *(H2 O)
HELIX 1 1 THR A 20 LEU A 25 1 6
HELIX 2 2 GLU A 84 MET A 89 1 6
HELIX 3 3 MET A 106 TYR A 119 1 14
HELIX 4 4 ARG A 136 ASN A 150 1 15
HELIX 5 5 THR A 184 VAL A 194 1 11
HELIX 6 6 THR A 327 ASN A 342 1 16
HELIX 7 7 GLY A 362 ARG A 375 1 14
HELIX 8 8 HIS A 411 ARG A 422 1 12
HELIX 9 9 ARG A 446 LEU A 448 5 3
HELIX 10 10 GLY A 450 THR A 459 1 10
HELIX 11 11 VAL A 497 GLN A 505 1 9
HELIX 12 12 THR A 564 GLU A 570 1 7
HELIX 13 13 ASN A 595 ASN A 601 1 7
SHEET 1 AA 6 LEU A 57 ASN A 60 0
SHEET 2 AA 6 TYR A 68 THR A 75 -1 O TYR A 68 N ASN A 60
SHEET 3 AA 6 ILE A 8 ILE A 11 1 O ILE A 8 N VAL A 73
SHEET 4 AA 6 SER A 94 ASP A 100 1 O SER A 94 N ALA A 9
SHEET 5 AA 6 VAL A 125 ASN A 128 1 O VAL A 126 N VAL A 99
SHEET 6 AA 6 VAL A 163 TYR A 164 1 O VAL A 163 N ILE A 127
SHEET 1 AB 7 THR A 238 ILE A 239 0
SHEET 2 AB 7 THR A 287 CYS A 289 -1 O CYS A 289 N THR A 238
SHEET 3 AB 7 GLN A 206 ILE A 209 -1 O MET A 207 N VAL A 288
SHEET 4 AB 7 GLY A 224 ARG A 228 -1 O ARG A 225 N GLN A 208
SHEET 5 AB 7 ALA A 270 ILE A 273 -1 O GLY A 271 N GLY A 224
SHEET 6 AB 7 VAL A 251 LEU A 255 -1 O GLY A 252 N ASP A 272
SHEET 7 AB 7 LEU A 258 GLU A 261 -1 O LEU A 258 N LEU A 255
SHEET 1 AC 2 ASP A 213 ASN A 215 0
SHEET 2 AC 2 GLY A 219 ILE A 221 -1 O GLY A 219 N ASN A 215
SHEET 1 AD 6 LEU A 345 GLU A 349 0
SHEET 2 AD 6 ALA A 355 GLY A 360 -1 O ARG A 357 N GLU A 348
SHEET 3 AD 6 VAL A 307 VAL A 313 -1 O VAL A 307 N GLY A 360
SHEET 4 AD 6 LEU A 380 VAL A 382 -1 O ALA A 381 N CYS A 312
SHEET 5 AD 6 GLU A 576 VAL A 580 -1 O VAL A 578 N VAL A 382
SHEET 6 AD 6 ILE A 585 LYS A 589 -1 O ARG A 586 N GLU A 579
SHEET 1 AE 4 LEU A 345 GLU A 349 0
SHEET 2 AE 4 ALA A 355 GLY A 360 -1 O ARG A 357 N GLU A 348
SHEET 3 AE 4 VAL A 307 VAL A 313 -1 O VAL A 307 N GLY A 360
SHEET 4 AE 4 LYS A 386 VAL A 387 -1 O LYS A 386 N SER A 308
SHEET 1 AF 4 ASP A 425 ASN A 428 0
SHEET 2 AF 4 ARG A 436 PRO A 444 -1 O ASP A 440 N LYS A 427
SHEET 3 AF 4 GLU A 398 GLU A 408 -1 O GLU A 401 N ILE A 443
SHEET 4 AF 4 LEU A 464 ASP A 473 -1 O LEU A 464 N ASP A 406
SHEET 1 AG 2 LEU A 488 SER A 490 0
SHEET 2 AG 2 LEU A 533 VAL A 535 1 O LEU A 533 N ILE A 489
CISPEP 1 THR A 19 THR A 20 0 0.05
CISPEP 2 SER A 29 GLY A 30 0 -2.27
CISPEP 3 LYS A 50 GLU A 51 0 0.05
CISPEP 4 ARG A 52 GLY A 53 0 0.01
CISPEP 5 ILE A 54 THR A 55 0 -0.04
CISPEP 6 ALA A 153 THR A 154 0 -0.01
CISPEP 7 GLU A 156 GLN A 157 0 -0.02
CISPEP 8 LEU A 158 ASP A 159 0 -0.04
CISPEP 9 PHE A 160 PRO A 161 0 0.04
CISPEP 10 HIS A 176 GLU A 177 0 -0.01
CISPEP 11 GLU A 177 ASP A 178 0 -0.02
CISPEP 12 ASP A 178 MET A 179 0 0.05
CISPEP 13 GLU A 295 ALA A 296 0 0.05
CISPEP 14 LEU A 300 SER A 301 0 -0.06
CISPEP 15 ARG A 476 PRO A 477 0 0.01
CISPEP 16 GLN A 484 ASN A 485 0 -0.01
SITE 1 AC1 9 HIS A 16 GLY A 17 LYS A 18 THR A 19
SITE 2 AC1 9 THR A 20 ASN A 128 LYS A 129 SER A 166
SITE 3 AC1 9 ALA A 167
CRYST1 241.946 241.946 241.946 90.00 90.00 90.00 I 41 3 2 48
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 0.004133 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004133 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004133 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
