HEADER CELL CYCLE 04-SEP-07 2VAW
TITLE FTSZ PSEUDOMONAS AERUGINOSA GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN FTSZ;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FTSZ;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 ATCC: 47053;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21AI(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS BACTERIAL CELL DIVISION PROTEIN, TUBULIN HOMOLOG, NUCLEOTIDE-BINDING,
KEYWDS 2 GTPASE, SEPTATION, CYTOPLASM, CELL CYCLE, GTP-BINDING, CELL
KEYWDS 3 DIVISION, POLYMERIZATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.OLIVA,J.LOWE
REVDAT 5 13-DEC-23 2VAW 1 REMARK
REVDAT 4 22-MAY-19 2VAW 1 REMARK
REVDAT 3 24-FEB-09 2VAW 1 VERSN
REVDAT 2 23-OCT-07 2VAW 1 JRNL
REVDAT 1 11-SEP-07 2VAW 0
JRNL AUTH M.A.OLIVA,D.TRAMBAIOLO,J.LOWE
JRNL TITL STRUCTURAL INSIGHTS INTO THE CONFORMATIONAL VARIABILITY OF
JRNL TITL 2 FTSZ
JRNL REF J.MOL.BIOL. V. 373 1229 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17900614
JRNL DOI 10.1016/J.JMB.2007.08.056
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 8573
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) : 0.206
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400
REMARK 3 FREE R VALUE TEST SET COUNT : 462
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 : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 894
REMARK 3 BIN R VALUE (WORKING SET) : 0.3197
REMARK 3 BIN FREE R VALUE : 0.3589
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 62
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 : 2277
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 26
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.51600
REMARK 3 B22 (A**2) : 4.51600
REMARK 3 B33 (A**2) : -9.03200
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) : 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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.357
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 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 : 0.35
REMARK 3 BSOL : 44.53
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 : GDP.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : 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
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2VAW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1290033674.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8626
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.76
REMARK 200 R MERGE FOR SHELL (I) : 0.16000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.160
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 1OFU
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 5.8, 26% PEG2000MME
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.15950
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.15950
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 33.15950
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: PQS
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 MET A 1
REMARK 465 GLY A 317
REMARK 465 ALA A 318
REMARK 465 ARG A 319
REMARK 465 LEU A 320
REMARK 465 GLU A 321
REMARK 465 LYS A 322
REMARK 465 PRO A 323
REMARK 465 VAL A 324
REMARK 465 LYS A 325
REMARK 465 VAL A 326
REMARK 465 VAL A 327
REMARK 465 ASP A 328
REMARK 465 ASN A 329
REMARK 465 THR A 330
REMARK 465 VAL A 331
REMARK 465 GLN A 332
REMARK 465 GLY A 333
REMARK 465 SER A 334
REMARK 465 ALA A 335
REMARK 465 ALA A 336
REMARK 465 GLN A 337
REMARK 465 ALA A 338
REMARK 465 ALA A 339
REMARK 465 ALA A 340
REMARK 465 PRO A 341
REMARK 465 ALA A 342
REMARK 465 GLN A 343
REMARK 465 ARG A 344
REMARK 465 GLU A 345
REMARK 465 GLN A 346
REMARK 465 GLN A 347
REMARK 465 SER A 348
REMARK 465 VAL A 349
REMARK 465 ASN A 350
REMARK 465 TYR A 351
REMARK 465 ARG A 352
REMARK 465 ASP A 353
REMARK 465 LEU A 354
REMARK 465 ASP A 355
REMARK 465 ARG A 356
REMARK 465 PRO A 357
REMARK 465 THR A 358
REMARK 465 VAL A 359
REMARK 465 MET A 360
REMARK 465 ARG A 361
REMARK 465 ASN A 362
REMARK 465 GLN A 363
REMARK 465 SER A 364
REMARK 465 HIS A 365
REMARK 465 GLY A 366
REMARK 465 SER A 367
REMARK 465 ALA A 368
REMARK 465 ALA A 369
REMARK 465 THR A 370
REMARK 465 ALA A 371
REMARK 465 ALA A 372
REMARK 465 LYS A 373
REMARK 465 LEU A 374
REMARK 465 ASN A 375
REMARK 465 PRO A 376
REMARK 465 GLN A 377
REMARK 465 ASP A 378
REMARK 465 ASP A 379
REMARK 465 LEU A 380
REMARK 465 ASP A 381
REMARK 465 TYR A 382
REMARK 465 LEU A 383
REMARK 465 ASP A 384
REMARK 465 ILE A 385
REMARK 465 PRO A 386
REMARK 465 ALA A 387
REMARK 465 PHE A 388
REMARK 465 LEU A 389
REMARK 465 ARG A 390
REMARK 465 ARG A 391
REMARK 465 GLN A 392
REMARK 465 ALA A 393
REMARK 465 ASP A 394
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 9 -120.49 -48.78
REMARK 500 ALA A 12 123.78 -37.50
REMARK 500 LYS A 32 54.86 -68.50
REMARK 500 ASN A 33 -156.28 -162.98
REMARK 500 ASN A 34 61.51 -100.09
REMARK 500 ALA A 47 -38.63 -36.92
REMARK 500 ASN A 52 83.92 54.40
REMARK 500 ALA A 54 -78.06 -43.17
REMARK 500 ALA A 55 128.33 -32.17
REMARK 500 ALA A 71 99.22 -39.71
REMARK 500 ALA A 73 12.42 48.94
REMARK 500 THR A 109 -72.75 -57.02
REMARK 500 VAL A 120 -74.12 -56.80
REMARK 500 MET A 124 -1.55 -59.13
REMARK 500 PRO A 135 149.80 -31.29
REMARK 500 PHE A 138 18.44 -67.48
REMARK 500 SER A 157 37.98 -141.79
REMARK 500 ILE A 172 -90.22 -47.78
REMARK 500 LEU A 173 -56.11 -17.27
REMARK 500 ASP A 176 9.18 -65.56
REMARK 500 SER A 178 138.14 -176.27
REMARK 500 LEU A 179 -57.32 -27.24
REMARK 500 ARG A 203 58.49 -119.77
REMARK 500 PRO A 204 151.62 -48.54
REMARK 500 ASP A 210 -168.95 -112.85
REMARK 500 THR A 216 -72.47 -52.73
REMARK 500 GLU A 220 51.71 31.75
REMARK 500 MET A 223 98.55 61.02
REMARK 500 CYS A 230 85.25 -153.14
REMARK 500 ALA A 237 -79.50 -63.50
REMARK 500 ARG A 246 5.75 -65.81
REMARK 500 LEU A 249 -3.30 -55.05
REMARK 500 LEU A 271 101.36 -49.29
REMARK 500 GLU A 284 -16.60 -44.30
REMARK 500 GLU A 289 -27.11 -36.70
REMARK 500 ASP A 302 39.42 -57.18
REMARK 500 ARG A 304 -124.78 -107.19
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 A1317
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OFU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SULA:FTSZ FROM PSEUDOMONAS AERUGINOSA
DBREF 2VAW A 1 394 UNP P47204 FTSZ_PSEAE 1 394
SEQRES 1 A 394 MET PHE GLU LEU VAL ASP ASN ILE ALA GLN THR ALA VAL
SEQRES 2 A 394 ILE LYS VAL ILE GLY VAL GLY GLY GLY GLY GLY ASN ALA
SEQRES 3 A 394 VAL ASN HIS MET ALA LYS ASN ASN VAL GLU GLY VAL GLU
SEQRES 4 A 394 PHE ILE CYS ALA ASN THR ASP ALA GLN ALA LEU LYS ASN
SEQRES 5 A 394 ILE ALA ALA ARG THR VAL LEU GLN LEU GLY PRO GLY VAL
SEQRES 6 A 394 THR LYS GLY LEU GLY ALA GLY ALA ASN PRO GLU VAL GLY
SEQRES 7 A 394 ARG GLN ALA ALA LEU GLU ASP ARG GLU ARG ILE SER GLU
SEQRES 8 A 394 VAL LEU GLU GLY ALA ASP MET VAL PHE ILE THR THR GLY
SEQRES 9 A 394 MET GLY GLY GLY THR GLY THR GLY ALA ALA PRO ILE ILE
SEQRES 10 A 394 ALA GLU VAL ALA LYS GLU MET GLY ILE LEU THR VAL ALA
SEQRES 11 A 394 VAL VAL THR ARG PRO PHE PRO PHE GLU GLY ARG LYS ARG
SEQRES 12 A 394 MET GLN ILE ALA ASP GLU GLY ILE ARG ALA LEU ALA GLU
SEQRES 13 A 394 SER VAL ASP SER LEU ILE THR ILE PRO ASN GLU LYS LEU
SEQRES 14 A 394 LEU THR ILE LEU GLY LYS ASP ALA SER LEU LEU ALA ALA
SEQRES 15 A 394 PHE ALA LYS ALA ASP ASP VAL LEU ALA GLY ALA VAL ARG
SEQRES 16 A 394 GLY ILE SER ASP ILE ILE LYS ARG PRO GLY MET ILE ASN
SEQRES 17 A 394 VAL ASP PHE ALA ASP VAL LYS THR VAL MET SER GLU MET
SEQRES 18 A 394 GLY MET ALA MET MET GLY THR GLY CYS ALA SER GLY PRO
SEQRES 19 A 394 ASN ARG ALA ARG GLU ALA THR GLU ALA ALA ILE ARG ASN
SEQRES 20 A 394 PRO LEU LEU GLU ASP VAL ASN LEU GLN GLY ALA ARG GLY
SEQRES 21 A 394 ILE LEU VAL ASN ILE THR ALA GLY PRO ASP LEU SER LEU
SEQRES 22 A 394 GLY GLU TYR SER ASP VAL GLY ASN ILE ILE GLU GLN PHE
SEQRES 23 A 394 ALA SER GLU HIS ALA THR VAL LYS VAL GLY THR VAL ILE
SEQRES 24 A 394 ASP ALA ASP MET ARG ASP GLU LEU HIS VAL THR VAL VAL
SEQRES 25 A 394 ALA THR GLY LEU GLY ALA ARG LEU GLU LYS PRO VAL LYS
SEQRES 26 A 394 VAL VAL ASP ASN THR VAL GLN GLY SER ALA ALA GLN ALA
SEQRES 27 A 394 ALA ALA PRO ALA GLN ARG GLU GLN GLN SER VAL ASN TYR
SEQRES 28 A 394 ARG ASP LEU ASP ARG PRO THR VAL MET ARG ASN GLN SER
SEQRES 29 A 394 HIS GLY SER ALA ALA THR ALA ALA LYS LEU ASN PRO GLN
SEQRES 30 A 394 ASP ASP LEU ASP TYR LEU ASP ILE PRO ALA PHE LEU ARG
SEQRES 31 A 394 ARG GLN ALA ASP
HET GDP A1317 28
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 GDP C10 H15 N5 O11 P2
FORMUL 3 HOH *26(H2 O)
HELIX 1 1 GLY A 20 LYS A 32 1 13
HELIX 2 2 GLY A 62 LYS A 67 1 6
HELIX 3 3 ASN A 74 ASP A 85 1 12
HELIX 4 4 ASP A 85 GLU A 94 1 10
HELIX 5 5 GLY A 108 GLY A 125 1 18
HELIX 6 6 PHE A 136 PHE A 138 5 3
HELIX 7 7 GLU A 139 GLU A 156 1 18
HELIX 8 8 ASN A 166 GLY A 174 1 9
HELIX 9 9 LYS A 175 ALA A 177 5 3
HELIX 10 10 SER A 178 ARG A 203 1 26
HELIX 11 11 ASP A 210 SER A 219 1 10
HELIX 12 12 ASN A 235 ARG A 246 1 12
HELIX 13 13 ASN A 247 GLU A 251 5 5
HELIX 14 14 SER A 272 ALA A 287 1 16
SHEET 1 AA 6 VAL A 58 GLN A 60 0
SHEET 2 AA 6 VAL A 38 ASN A 44 1 O CYS A 42 N LEU A 59
SHEET 3 AA 6 ILE A 14 VAL A 19 1 O ILE A 14 N GLU A 39
SHEET 4 AA 6 MET A 98 GLY A 104 1 O MET A 98 N LYS A 15
SHEET 5 AA 6 LEU A 127 ARG A 134 1 O LEU A 127 N VAL A 99
SHEET 6 AA 6 SER A 160 PRO A 165 1 O SER A 160 N ALA A 130
SHEET 1 AB 4 MET A 225 ALA A 231 0
SHEET 2 AB 4 LEU A 307 THR A 314 -1 O LEU A 307 N ALA A 231
SHEET 3 AB 4 GLY A 260 ALA A 267 -1 O GLY A 260 N THR A 314
SHEET 4 AB 4 THR A 292 ILE A 299 1 O THR A 292 N ILE A 261
SITE 1 AC1 17 GLY A 20 GLY A 21 GLY A 22 ASN A 25
SITE 2 AC1 17 GLY A 104 MET A 105 GLY A 107 GLY A 108
SITE 3 AC1 17 THR A 109 GLY A 110 GLU A 139 ARG A 143
SITE 4 AC1 17 PHE A 183 ALA A 186 ASP A 187 HOH A2025
SITE 5 AC1 17 HOH A2026
CRYST1 100.658 100.658 66.319 90.00 90.00 120.00 P 63 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 0.009935 0.005736 0.000000 0.00000
SCALE2 0.000000 0.011472 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015079 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
