HEADER SIGNALING PROTEIN 04-JUN-06 2H7V
TITLE CO-CRYSTAL STRUCTURE OF YPKA-RAC1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MIGRATION-INDUCING PROTEIN 5;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1, ISOFORM RAC1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN KINASE YPKA;
COMPND 9 CHAIN: C, D;
COMPND 10 SYNONYM: PROTEIN KINASE A, TARGETED EFFECTOR PROTEIN KINASE;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MIG5, RAC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T3;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: YERSINIA PSEUDOTUBERCULOSIS;
SOURCE 13 ORGANISM_TAXID: 633;
SOURCE 14 GENE: YPKA;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PGEX4T3
KEYWDS YPKA, YOPO, RAC1, GDI, GTPASE, YERSINIA, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PREHNA,M.IVANOV,J.B.BLISKA,C.E.STEBBINS
REVDAT 3 13-JUL-11 2H7V 1 VERSN
REVDAT 2 24-FEB-09 2H7V 1 VERSN
REVDAT 1 19-SEP-06 2H7V 0
JRNL AUTH G.PREHNA,M.I.IVANOV,J.B.BLISKA,C.E.STEBBINS
JRNL TITL YERSINIA VIRULENCE DEPENDS ON MIMICRY OF HOST RHO-FAMILY
JRNL TITL 2 NUCLEOTIDE DISSOCIATION INHIBITORS.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 126 869 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 16959567
JRNL DOI 10.1016/J.CELL.2006.06.056
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 51262
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2552
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3649
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.3730
REMARK 3 BIN FREE R VALUE SET COUNT : 162
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7058
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 75
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.30000
REMARK 3 B22 (A**2) : 0.97000
REMARK 3 B33 (A**2) : -5.70000
REMARK 3 B12 (A**2) : 4.77000
REMARK 3 B13 (A**2) : -3.29000
REMARK 3 B23 (A**2) : -0.77000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.354
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.261
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.254
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.265
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7223 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6710 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9775 ; 1.666 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15624 ; 0.866 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 883 ; 7.039 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 318 ;35.492 ;24.308
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1340 ;19.171 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 53 ;17.951 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1147 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7826 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1367 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1914 ; 0.242 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7111 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3697 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4635 ; 0.093 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 203 ; 0.196 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.059 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.034 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 21 ; 0.219 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 109 ; 0.226 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.140 ; 0.200
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): 5686 ; 0.874 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1803 ; 0.136 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7200 ; 1.091 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3128 ; 1.579 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2575 ; 2.504 ; 4.500
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3250 -13.9150 -34.1240
REMARK 3 T TENSOR
REMARK 3 T11: -0.0837 T22: -0.3251
REMARK 3 T33: -0.1239 T12: 0.0965
REMARK 3 T13: -0.0052 T23: -0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 2.6988 L22: 6.4001
REMARK 3 L33: 4.5338 L12: -2.5200
REMARK 3 L13: 2.4130 L23: -2.4713
REMARK 3 S TENSOR
REMARK 3 S11: -0.2353 S12: -0.0195 S13: 0.3198
REMARK 3 S21: -0.1464 S22: -0.1275 S23: -0.5774
REMARK 3 S31: -0.4192 S32: 0.3443 S33: 0.3628
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 179
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4060 -13.5380 -98.9150
REMARK 3 T TENSOR
REMARK 3 T11: -0.0516 T22: -0.0891
REMARK 3 T33: -0.0465 T12: -0.0576
REMARK 3 T13: -0.0191 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 8.0317 L22: 1.3848
REMARK 3 L33: 3.3601 L12: -1.5120
REMARK 3 L13: 3.2496 L23: -0.5097
REMARK 3 S TENSOR
REMARK 3 S11: -0.2300 S12: 0.1122 S13: 0.9175
REMARK 3 S21: -0.0668 S22: -0.2511 S23: -0.1441
REMARK 3 S31: -0.7157 S32: 0.0197 S33: 0.4811
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 439 C 514
REMARK 3 RESIDUE RANGE : C 532 C 648
REMARK 3 RESIDUE RANGE : C 657 C 702
REMARK 3 RESIDUE RANGE : C 704 C 732
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2680 -37.5410 -71.3430
REMARK 3 T TENSOR
REMARK 3 T11: -0.0359 T22: -0.1176
REMARK 3 T33: -0.0211 T12: -0.0392
REMARK 3 T13: -0.0016 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.1446 L22: 1.1338
REMARK 3 L33: 6.6549 L12: 0.4021
REMARK 3 L13: -0.9244 L23: -2.6789
REMARK 3 S TENSOR
REMARK 3 S11: -0.1305 S12: 0.1575 S13: 0.0637
REMARK 3 S21: -0.0424 S22: 0.3416 S23: 0.0289
REMARK 3 S31: 0.7001 S32: 0.0917 S33: -0.2111
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 441 D 486
REMARK 3 RESIDUE RANGE : D 489 D 512
REMARK 3 RESIDUE RANGE : D 533 D 647
REMARK 3 RESIDUE RANGE : D 658 D 732
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9680 -4.6970 -56.5220
REMARK 3 T TENSOR
REMARK 3 T11: 0.2540 T22: 0.0845
REMARK 3 T33: 0.0071 T12: 0.0858
REMARK 3 T13: -0.0901 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 0.5454 L22: 4.1627
REMARK 3 L33: 7.7321 L12: 0.0415
REMARK 3 L13: -0.0440 L23: 5.6665
REMARK 3 S TENSOR
REMARK 3 S11: -0.0116 S12: 0.2689 S13: -0.2143
REMARK 3 S21: 0.6369 S22: -0.3275 S23: 0.2754
REMARK 3 S31: 0.7133 S32: -1.2313 S33: 0.3392
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
REMARK 4
REMARK 4 2H7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-06.
REMARK 100 THE RCSB ID CODE IS RCSB038039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-05; 21-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 80; NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X29A; X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1; 1.1
REMARK 200 MONOCHROMATOR : SI(111); SI(111)
REMARK 200 OPTICS : ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SAGITTAL FOCUSING MONOCHROMETER
REMARK 200 AND VERTICAL FOCUSING MIRROR;
REMARK 200 ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SAGITTAL FOCUSING MONOCHROMETER
REMARK 200 AND VERTICAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51987
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 95.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ID 2H7O, 1MH1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 6.5-7.5, 5%-8%
REMARK 280 PEGMME2000 MICRO SEEDING, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
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, 2
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 300 REMARK: DIMER CONSISTING OF ONE YPKA MOLECULE AND ONE RAC1
REMARK 300 MOLECULE. BIOLOGICAL CONTACT IS RESIDUES 574 TO 601 OF YPKA.
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 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 PRO A 179
REMARK 465 PRO A 180
REMARK 465 PRO A 181
REMARK 465 VAL A 182
REMARK 465 LYS A 183
REMARK 465 LYS A 184
REMARK 465 PRO B 180
REMARK 465 PRO B 181
REMARK 465 VAL B 182
REMARK 465 LYS B 183
REMARK 465 LYS B 184
REMARK 465 GLY C 430
REMARK 465 PRO C 431
REMARK 465 VAL C 432
REMARK 465 ASP C 433
REMARK 465 SER C 434
REMARK 465 THR C 435
REMARK 465 ASP C 436
REMARK 465 VAL C 437
REMARK 465 ARG C 438
REMARK 465 ARG C 515
REMARK 465 GLU C 516
REMARK 465 GLY C 517
REMARK 465 ASP C 518
REMARK 465 THR C 519
REMARK 465 LYS C 520
REMARK 465 ASN C 521
REMARK 465 SER C 522
REMARK 465 SER C 523
REMARK 465 THR C 524
REMARK 465 GLU C 525
REMARK 465 VAL C 526
REMARK 465 SER C 527
REMARK 465 PRO C 528
REMARK 465 TYR C 529
REMARK 465 HIS C 530
REMARK 465 ARG C 531
REMARK 465 VAL C 649
REMARK 465 VAL C 650
REMARK 465 LYS C 651
REMARK 465 PHE C 652
REMARK 465 GLY C 653
REMARK 465 THR C 654
REMARK 465 GLU C 655
REMARK 465 GLN C 656
REMARK 465 GLY D 430
REMARK 465 PRO D 431
REMARK 465 VAL D 432
REMARK 465 ASP D 433
REMARK 465 SER D 434
REMARK 465 THR D 435
REMARK 465 ASP D 436
REMARK 465 VAL D 437
REMARK 465 ARG D 438
REMARK 465 ARG D 439
REMARK 465 ILE D 440
REMARK 465 GLY D 487
REMARK 465 GLY D 488
REMARK 465 LYS D 513
REMARK 465 GLY D 514
REMARK 465 ARG D 515
REMARK 465 GLU D 516
REMARK 465 GLY D 517
REMARK 465 ASP D 518
REMARK 465 THR D 519
REMARK 465 LYS D 520
REMARK 465 ASN D 521
REMARK 465 SER D 522
REMARK 465 SER D 523
REMARK 465 THR D 524
REMARK 465 GLU D 525
REMARK 465 VAL D 526
REMARK 465 SER D 527
REMARK 465 PRO D 528
REMARK 465 TYR D 529
REMARK 465 HIS D 530
REMARK 465 ARG D 531
REMARK 465 SER D 532
REMARK 465 PRO D 648
REMARK 465 VAL D 649
REMARK 465 VAL D 650
REMARK 465 LYS D 651
REMARK 465 PHE D 652
REMARK 465 GLY D 653
REMARK 465 THR D 654
REMARK 465 GLU D 655
REMARK 465 GLN D 656
REMARK 465 TYR D 657
REMARK 465 MET D 703
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 OE1 GLU C 709 O HOH C 30 2.16
REMARK 500 OG1 THR D 658 ND1 HIS D 661 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 62 CG GLU B 62 CD 0.103
REMARK 500 CYS B 81 CB CYS B 81 SG -0.111
REMARK 500 CYS B 105 CB CYS B 105 SG -0.109
REMARK 500 SER C 629 C SER C 629 O 0.153
REMARK 500 GLY C 630 N GLY C 630 CA -0.124
REMARK 500 GLU D 728 CB GLU D 728 CG 0.117
REMARK 500 GLU D 728 CG GLU D 728 CD 0.107
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 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 68 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 LEU B 134 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG C 628 NE - CZ - NH1 ANGL. DEV. = 3.0 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 TYR A 32 124.08 57.21
REMARK 500 GLN A 61 -81.15 170.16
REMARK 500 GLU A 62 -53.51 -165.05
REMARK 500 LYS A 96 -57.43 -127.66
REMARK 500 LYS A 132 43.90 -142.94
REMARK 500 PRO A 136 154.96 -49.20
REMARK 500 SER B 2B -147.96 -73.74
REMARK 500 LYS B 1A 113.13 67.05
REMARK 500 ASN B 26 14.56 57.02
REMARK 500 TYR B 32 108.73 50.49
REMARK 500 ALA B 59 -6.80 -147.29
REMARK 500 GLN B 61 64.47 -169.01
REMARK 500 ASP B 63 -40.32 146.84
REMARK 500 SER B 86 78.99 -155.35
REMARK 500 LYS B 96 -53.04 -133.22
REMARK 500 LYS B 133 60.24 28.25
REMARK 500 LEU C 464 117.12 -37.40
REMARK 500 GLU C 486 36.83 -153.89
REMARK 500 GLN C 581 71.13 -56.81
REMARK 500 GLN C 582 -40.25 151.06
REMARK 500 GLN C 584 178.61 57.18
REMARK 500 ALA C 633 -50.17 -27.22
REMARK 500 ARG C 647 90.91 -172.37
REMARK 500 GLU C 678 -14.40 -48.96
REMARK 500 THR C 680 -54.10 -27.35
REMARK 500 LEU C 702 73.53 -102.74
REMARK 500 LYS D 462 71.29 41.81
REMARK 500 ASP D 492 10.43 -60.55
REMARK 500 PHE D 534 -33.12 -159.91
REMARK 500 MET D 535 -39.91 -34.69
REMARK 500 LEU D 536 -73.35 -40.99
REMARK 500 GLN D 552 -128.24 79.19
REMARK 500 THR D 553 91.37 54.62
REMARK 500 GLN D 584 142.98 72.49
REMARK 500 PRO D 585 83.34 -27.94
REMARK 500 VAL D 586 133.55 -39.52
REMARK 500 SER D 645 106.33 -55.63
REMARK 500 THR D 646 8.12 42.44
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 ARG C 485 GLU C 486 146.46
REMARK 500 GLY C 630 SER C 631 141.91
REMARK 500 ASP D 551 GLN D 552 134.20
REMARK 500 GLN D 552 THR D 553 -148.46
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 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 35 O
REMARK 620 2 THR A 17 OG1 74.4
REMARK 620 3 GDP A 200 O1B 158.3 126.7
REMARK 620 4 GDP A 200 O3B 146.1 71.7 55.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 17 OG1
REMARK 620 2 GDP B 200 O3B 85.7
REMARK 620 3 GDP B 200 O1B 135.0 49.3
REMARK 620 4 THR B 35 O 78.2 146.8 139.8
REMARK 620 N 1 2 3
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2H7O RELATED DB: PDB
DBREF 2H7V A 1 184 UNP P63000 RAC1_HUMAN 1 184
DBREF 2H7V B 1 184 UNP P63000 RAC1_HUMAN 1 184
DBREF 2H7V C 434 732 UNP Q05608 YPKA_YERPS 434 732
DBREF 2H7V D 434 732 UNP Q05608 YPKA_YERPS 434 732
SEQADV 2H7V GLY A 1B UNP P63000 CLONING ARTIFACT
SEQADV 2H7V SER A 2B UNP P63000 CLONING ARTIFACT
SEQADV 2H7V LYS A 1A UNP P63000 CLONING ARTIFACT
SEQADV 2H7V LEU A 2A UNP P63000 CLONING ARTIFACT
SEQADV 2H7V SER A 78 UNP P63000 PHE 78 ENGINEERED
SEQADV 2H7V GLY B 1B UNP P63000 CLONING ARTIFACT
SEQADV 2H7V SER B 2B UNP P63000 CLONING ARTIFACT
SEQADV 2H7V LYS B 1A UNP P63000 CLONING ARTIFACT
SEQADV 2H7V LEU B 2A UNP P63000 CLONING ARTIFACT
SEQADV 2H7V SER B 78 UNP P63000 PHE 78 ENGINEERED
SEQADV 2H7V GLY C 430 UNP Q05608 CLONING ARTIFACT
SEQADV 2H7V PRO C 431 UNP Q05608 CLONING ARTIFACT
SEQADV 2H7V VAL C 432 UNP Q05608 CLONING ARTIFACT
SEQADV 2H7V ASP C 433 UNP Q05608 CLONING ARTIFACT
SEQADV 2H7V GLY D 430 UNP Q05608 CLONING ARTIFACT
SEQADV 2H7V PRO D 431 UNP Q05608 CLONING ARTIFACT
SEQADV 2H7V VAL D 432 UNP Q05608 CLONING ARTIFACT
SEQADV 2H7V ASP D 433 UNP Q05608 CLONING ARTIFACT
SEQRES 1 A 188 GLY SER LYS LEU MET GLN ALA ILE LYS CYS VAL VAL VAL
SEQRES 2 A 188 GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER
SEQRES 3 A 188 TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR
SEQRES 4 A 188 VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY
SEQRES 5 A 188 LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN
SEQRES 6 A 188 GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN
SEQRES 7 A 188 THR ASP VAL SER LEU ILE CYS PHE SER LEU VAL SER PRO
SEQRES 8 A 188 ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU
SEQRES 9 A 188 VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL
SEQRES 10 A 188 GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE
SEQRES 11 A 188 GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR
SEQRES 12 A 188 PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL
SEQRES 13 A 188 LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU
SEQRES 14 A 188 LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS
SEQRES 15 A 188 PRO PRO PRO VAL LYS LYS
SEQRES 1 B 188 GLY SER LYS LEU MET GLN ALA ILE LYS CYS VAL VAL VAL
SEQRES 2 B 188 GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER
SEQRES 3 B 188 TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR
SEQRES 4 B 188 VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY
SEQRES 5 B 188 LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN
SEQRES 6 B 188 GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN
SEQRES 7 B 188 THR ASP VAL SER LEU ILE CYS PHE SER LEU VAL SER PRO
SEQRES 8 B 188 ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU
SEQRES 9 B 188 VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL
SEQRES 10 B 188 GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE
SEQRES 11 B 188 GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR
SEQRES 12 B 188 PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL
SEQRES 13 B 188 LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU
SEQRES 14 B 188 LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS
SEQRES 15 B 188 PRO PRO PRO VAL LYS LYS
SEQRES 1 C 303 GLY PRO VAL ASP SER THR ASP VAL ARG ARG ILE THR PRO
SEQRES 2 C 303 LYS LYS LEU ARG GLU LEU SER ASP LEU LEU ARG THR HIS
SEQRES 3 C 303 LEU SER SER ALA ALA THR LYS GLN LEU ASP MET GLY GLY
SEQRES 4 C 303 VAL LEU SER ASP LEU ASP THR MET LEU VAL ALA LEU ASP
SEQRES 5 C 303 LYS ALA GLU ARG GLU GLY GLY VAL ASP LYS ASP GLN LEU
SEQRES 6 C 303 LYS SER PHE ASN SER LEU ILE LEU LYS THR TYR ARG VAL
SEQRES 7 C 303 ILE GLU ASP TYR VAL LYS GLY ARG GLU GLY ASP THR LYS
SEQRES 8 C 303 ASN SER SER THR GLU VAL SER PRO TYR HIS ARG SER ASN
SEQRES 9 C 303 PHE MET LEU SER ILE VAL GLU PRO SER LEU GLN ARG ILE
SEQRES 10 C 303 GLN LYS HIS LEU ASP GLN THR HIS SER PHE SER ASP ILE
SEQRES 11 C 303 GLY SER LEU VAL ARG ALA HIS LYS HIS LEU GLU THR LEU
SEQRES 12 C 303 LEU GLU VAL LEU VAL THR LEU SER GLN GLN GLY GLN PRO
SEQRES 13 C 303 VAL SER SER GLU THR TYR GLY PHE LEU ASN ARG LEU ALA
SEQRES 14 C 303 GLU ALA LYS ILE THR LEU SER GLN GLN LEU ASN THR LEU
SEQRES 15 C 303 GLN GLN GLN GLN GLU SER ALA LYS ALA GLN LEU SER ILE
SEQRES 16 C 303 LEU ILE ASN ARG SER GLY SER TRP ALA ASP VAL ALA ARG
SEQRES 17 C 303 GLN SER LEU GLN ARG PHE ASP SER THR ARG PRO VAL VAL
SEQRES 18 C 303 LYS PHE GLY THR GLU GLN TYR THR ALA ILE HIS ARG GLN
SEQRES 19 C 303 MET MET ALA ALA HIS ALA ALA ILE THR LEU GLN GLU VAL
SEQRES 20 C 303 SER GLU PHE THR ASP ASP MET ARG ASN PHE THR VAL ASP
SEQRES 21 C 303 SER ILE PRO LEU LEU ILE GLN LEU GLY ARG SER SER LEU
SEQRES 22 C 303 MET ASP GLU HIS LEU VAL GLU GLN ARG GLU LYS LEU ARG
SEQRES 23 C 303 GLU LEU THR THR ILE ALA GLU ARG LEU ASN ARG LEU GLU
SEQRES 24 C 303 ARG GLU TRP MET
SEQRES 1 D 303 GLY PRO VAL ASP SER THR ASP VAL ARG ARG ILE THR PRO
SEQRES 2 D 303 LYS LYS LEU ARG GLU LEU SER ASP LEU LEU ARG THR HIS
SEQRES 3 D 303 LEU SER SER ALA ALA THR LYS GLN LEU ASP MET GLY GLY
SEQRES 4 D 303 VAL LEU SER ASP LEU ASP THR MET LEU VAL ALA LEU ASP
SEQRES 5 D 303 LYS ALA GLU ARG GLU GLY GLY VAL ASP LYS ASP GLN LEU
SEQRES 6 D 303 LYS SER PHE ASN SER LEU ILE LEU LYS THR TYR ARG VAL
SEQRES 7 D 303 ILE GLU ASP TYR VAL LYS GLY ARG GLU GLY ASP THR LYS
SEQRES 8 D 303 ASN SER SER THR GLU VAL SER PRO TYR HIS ARG SER ASN
SEQRES 9 D 303 PHE MET LEU SER ILE VAL GLU PRO SER LEU GLN ARG ILE
SEQRES 10 D 303 GLN LYS HIS LEU ASP GLN THR HIS SER PHE SER ASP ILE
SEQRES 11 D 303 GLY SER LEU VAL ARG ALA HIS LYS HIS LEU GLU THR LEU
SEQRES 12 D 303 LEU GLU VAL LEU VAL THR LEU SER GLN GLN GLY GLN PRO
SEQRES 13 D 303 VAL SER SER GLU THR TYR GLY PHE LEU ASN ARG LEU ALA
SEQRES 14 D 303 GLU ALA LYS ILE THR LEU SER GLN GLN LEU ASN THR LEU
SEQRES 15 D 303 GLN GLN GLN GLN GLU SER ALA LYS ALA GLN LEU SER ILE
SEQRES 16 D 303 LEU ILE ASN ARG SER GLY SER TRP ALA ASP VAL ALA ARG
SEQRES 17 D 303 GLN SER LEU GLN ARG PHE ASP SER THR ARG PRO VAL VAL
SEQRES 18 D 303 LYS PHE GLY THR GLU GLN TYR THR ALA ILE HIS ARG GLN
SEQRES 19 D 303 MET MET ALA ALA HIS ALA ALA ILE THR LEU GLN GLU VAL
SEQRES 20 D 303 SER GLU PHE THR ASP ASP MET ARG ASN PHE THR VAL ASP
SEQRES 21 D 303 SER ILE PRO LEU LEU ILE GLN LEU GLY ARG SER SER LEU
SEQRES 22 D 303 MET ASP GLU HIS LEU VAL GLU GLN ARG GLU LYS LEU ARG
SEQRES 23 D 303 GLU LEU THR THR ILE ALA GLU ARG LEU ASN ARG LEU GLU
SEQRES 24 D 303 ARG GLU TRP MET
HET MG A 201 1
HET MG B 201 1
HET GDP A 200 28
HET GDP B 200 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 5 MG 2(MG 2+)
FORMUL 7 GDP 2(C10 H15 N5 O11 P2)
FORMUL 9 HOH *75(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 GLU A 62 ARG A 68 1 7
HELIX 3 3 PRO A 69 TYR A 72 5 4
HELIX 4 4 SER A 86 LYS A 96 1 11
HELIX 5 5 LYS A 96 CYS A 105 1 10
HELIX 6 6 LYS A 116 ASP A 121 5 6
HELIX 7 7 ASP A 122 GLU A 131 1 10
HELIX 8 8 THR A 138 ILE A 149 1 12
HELIX 9 9 GLY A 164 LEU A 177 1 14
HELIX 10 10 GLY B 15 ASN B 26 1 12
HELIX 11 11 ASP B 63 ARG B 68 1 6
HELIX 12 12 PRO B 69 TYR B 72 5 4
HELIX 13 13 SER B 86 LYS B 96 1 11
HELIX 14 14 LYS B 96 CYS B 105 1 10
HELIX 15 15 LYS B 116 ASP B 121 5 6
HELIX 16 16 ASP B 122 GLU B 131 1 10
HELIX 17 17 THR B 138 GLY B 150 1 13
HELIX 18 18 GLY B 164 CYS B 178 1 15
HELIX 19 19 THR C 441 THR C 461 1 21
HELIX 20 20 ASP C 465 ARG C 485 1 21
HELIX 21 21 ASP C 490 LYS C 513 1 24
HELIX 22 22 ASN C 533 LYS C 548 1 16
HELIX 23 23 ASP C 558 GLN C 581 1 24
HELIX 24 24 SER C 587 GLY C 630 1 44
HELIX 25 25 TRP C 632 SER C 645 1 14
HELIX 26 26 THR C 658 VAL C 676 1 19
HELIX 27 27 PHE C 679 GLY C 698 1 20
HELIX 28 28 ASP C 704 MET C 732 1 29
HELIX 29 29 LYS D 444 THR D 461 1 18
HELIX 30 30 ASP D 465 GLU D 484 1 20
HELIX 31 31 ASP D 490 ASP D 492 5 3
HELIX 32 32 GLN D 493 TYR D 511 1 19
HELIX 33 33 PHE D 534 VAL D 539 1 6
HELIX 34 34 VAL D 539 LEU D 550 1 12
HELIX 35 35 SER D 555 SER D 557 5 3
HELIX 36 36 ASP D 558 GLY D 583 1 26
HELIX 37 37 SER D 587 SER D 645 1 59
HELIX 38 38 THR D 658 VAL D 676 1 19
HELIX 39 39 PHE D 679 GLY D 698 1 20
HELIX 40 40 ASP D 704 MET D 732 1 29
SHEET 1 A 6 TYR A 40 VAL A 46 0
SHEET 2 A 6 LYS A 49 TRP A 56 -1 O LEU A 53 N ALA A 42
SHEET 3 A 6 GLN A 2 VAL A 9 1 N ILE A 4 O ASN A 52
SHEET 4 A 6 VAL A 77 SER A 83 1 O CYS A 81 N VAL A 9
SHEET 5 A 6 ILE A 110 THR A 115 1 O VAL A 113 N ILE A 80
SHEET 6 A 6 LYS A 153 GLU A 156 1 O LEU A 155 N LEU A 112
SHEET 1 B 6 TYR B 40 VAL B 44 0
SHEET 2 B 6 VAL B 51 TRP B 56 -1 O VAL B 51 N VAL B 44
SHEET 3 B 6 GLN B 2 GLY B 10 1 N ILE B 4 O GLY B 54
SHEET 4 B 6 VAL B 77 SER B 83 1 O CYS B 81 N VAL B 9
SHEET 5 B 6 ILE B 110 THR B 115 1 O THR B 115 N PHE B 82
SHEET 6 B 6 LYS B 153 GLU B 156 1 O LEU B 155 N LEU B 112
LINK MG MG A 201 O THR A 35 1555 1555 1.95
LINK MG MG A 201 OG1 THR A 17 1555 1555 2.37
LINK MG MG A 201 O1B GDP A 200 1555 1555 2.96
LINK MG MG A 201 O3B GDP A 200 1555 1555 2.53
LINK MG MG B 201 OG1 THR B 17 1555 1555 2.33
LINK MG MG B 201 O3B GDP B 200 1555 1555 2.10
LINK MG MG B 201 O1B GDP B 200 1555 1555 3.14
LINK MG MG B 201 O THR B 35 1555 1555 1.97
SITE 1 AC1 3 THR A 17 THR A 35 GDP A 200
SITE 1 AC2 3 THR B 17 THR B 35 GDP B 200
SITE 1 AC3 15 ASP A 11 ALA A 13 VAL A 14 GLY A 15
SITE 2 AC3 15 LYS A 16 THR A 17 CYS A 18 PHE A 28
SITE 3 AC3 15 ILE A 33 LYS A 116 ASP A 118 LEU A 119
SITE 4 AC3 15 ALA A 159 LEU A 160 MG A 201
SITE 1 AC4 15 ALA B 13 VAL B 14 GLY B 15 LYS B 16
SITE 2 AC4 15 THR B 17 CYS B 18 PHE B 28 ILE B 33
SITE 3 AC4 15 LYS B 116 ASP B 118 LEU B 119 SER B 158
SITE 4 AC4 15 ALA B 159 LEU B 160 MG B 201
CRYST1 66.398 75.519 99.772 92.08 103.38 115.79 P 1 2
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 0.015061 0.007277 0.004779 0.00000
SCALE2 0.000000 0.014707 0.002328 0.00000
SCALE3 0.000000 0.000000 0.010431 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
