HEADER STRUCTURAL PROTEIN 27-JUL-12 4B45
TITLE CETZ2 FROM HALOFERAX VOLCANII - GTPGS BOUND PROTOFILAMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN FTSZ;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-349;
COMPND 5 SYNONYM: CETZ2;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CHAIN A AND B REPRESENT FRAGMENTS OF A SINGLE
COMPND 8 MOLECULE;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CELL DIVISION PROTEIN FTSZ;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: RESIDUES 350-360;
COMPND 13 SYNONYM: CETZ2;
COMPND 14 ENGINEERED: YES;
COMPND 15 OTHER_DETAILS: CHAIN A AND B REPRESENT FRAGMENTS OF A SINGLE
COMPND 16 MOLECULE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOFERAX VOLCANII;
SOURCE 3 ORGANISM_TAXID: 2246;
SOURCE 4 ATCC: 29605;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHIS17;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HALOFERAX VOLCANII;
SOURCE 13 ORGANISM_TAXID: 2246;
SOURCE 14 ATCC: 29605;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHIS17
KEYWDS STRUCTURAL PROTEIN, TUBULIN, ARCHAEA, CYTOSKELETON, CELL SHAPE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.H.S.AYLETT,I.G.DUGGIN,J.LOWE
REVDAT 6 25-MAR-15 4B45 1 JRNL
REVDAT 5 14-JAN-15 4B45 1 JRNL REMARK
REVDAT 4 24-DEC-14 4B45 1 REMARK
REVDAT 3 17-DEC-14 4B45 1 JRNL
REVDAT 2 21-AUG-13 4B45 1 TITLE REMARK
REVDAT 1 14-AUG-13 4B45 0
JRNL AUTH I.G.DUGGIN,C.H.S.AYLETT,J.C.WALSH,K.A.MICHIE,Q.WANG,
JRNL AUTH 2 L.TURNBULL,E.M.DAWSON,E.J.HARRY,C.B.WHITCHURCH,A.AMOS,J.LOWE
JRNL TITL CETZ TUBULIN-LIKE PROTEINS CONTROL ARCHAEAL CELL SHAPE
JRNL REF NATURE V. 519 362 2015
JRNL REFN ISSN 0028-0836
JRNL PMID 25533961
JRNL DOI 10.1038/NATURE13983
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.100
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.284
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.24
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.65
REMARK 3 NUMBER OF REFLECTIONS : 20523
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1798
REMARK 3 R VALUE (WORKING SET) : 0.1771
REMARK 3 FREE R VALUE : 0.2280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1738
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.2914 - 4.8053 0.94 2679 155 0.1668 0.2109
REMARK 3 2 4.8053 - 3.8151 0.94 2751 128 0.1337 0.1367
REMARK 3 3 3.8151 - 3.3331 0.95 2712 155 0.1357 0.1821
REMARK 3 4 3.3331 - 3.0284 0.96 2709 131 0.1595 0.2261
REMARK 3 5 3.0284 - 2.8114 0.96 2763 145 0.1783 0.2603
REMARK 3 6 2.8114 - 2.6457 0.95 2751 130 0.1852 0.2506
REMARK 3 7 2.6457 - 2.5132 0.95 2714 170 0.2009 0.2561
REMARK 3 8 2.5132 - 2.4039 0.95 2713 126 0.2081 0.2590
REMARK 3 9 2.4039 - 2.3113 0.94 2724 158 0.2174 0.3029
REMARK 3 10 2.3113 - 2.2316 0.94 2662 145 0.2487 0.2639
REMARK 3 11 2.2316 - 2.1618 0.94 2654 158 0.2482 0.3366
REMARK 3 12 2.1618 - 2.1000 0.94 2688 137 0.2873 0.3747
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 1
REMARK 3 B_SOL : 1
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.20
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2559
REMARK 3 ANGLE : 1.091 3474
REMARK 3 CHIRALITY : 0.069 409
REMARK 3 PLANARITY : 0.004 460
REMARK 3 DIHEDRAL : 13.777 924
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A OR CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5484 -21.3657 -14.9165
REMARK 3 T TENSOR
REMARK 3 T11: 0.3346 T22: 0.3602
REMARK 3 T33: 0.3538 T12: 0.0151
REMARK 3 T13: -0.0003 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 1.0809 L22: 2.5708
REMARK 3 L33: 0.3070 L12: 0.6614
REMARK 3 L13: -0.0340 L23: -0.0511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0386 S12: -0.0340 S13: -0.0289
REMARK 3 S21: -0.0298 S22: -0.0326 S23: -0.0247
REMARK 3 S31: 0.0061 S32: -0.0349 S33: 0.0035
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CHAIN B REPRESENTS PART OF THE
REMARK 3 C-TERMINAL TAIL OF ANOTHER CETZ3 SUBUNIT, BUT HAS BEEN
REMARK 3 MODELED AS A SEPARATE CHAIN AS WE CANNOT BE CERTAIN FROM
REMARK 3 WHICH IT ORIGINATES FROM.
REMARK 4
REMARK 4 4B45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-12.
REMARK 100 THE PDBE ID CODE IS EBI-53530.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979500
REMARK 200 MONOCHROMATOR : GRAPHITE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : PSI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20523
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 40.28
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : 0.13
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 0.94
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.50
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: CETZ4 MODEL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.15 M AMMONIUM SULFATE, 0.1 M
REMARK 280 NA CITRATE PH 5
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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.2 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 THR A 200
REMARK 465 GLU A 201
REMARK 465 GLY A 202
REMARK 465 VAL A 203
REMARK 465 GLY A 204
REMARK 465 GLU A 205
REMARK 465 SER A 206
REMARK 465 GLU A 342
REMARK 465 PRO A 343
REMARK 465 ARG A 344
REMARK 465 GLU A 345
REMARK 465 ASP A 346
REMARK 465 PRO A 347
REMARK 465 LYS A 348
REMARK 465 GLY A 349
REMARK 465 HIS B 363
REMARK 465 HIS B 364
REMARK 465 HIS B 365
REMARK 465 HIS B 366
REMARK 465 HIS B 367
REMARK 465 HIS B 368
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 ND2 ASN A 68 OG SER A 109 2.18
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 122 -41.10 -145.55
REMARK 500 ASP B 355 157.79 73.01
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 GSP A1342
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4B46 RELATED DB: PDB
REMARK 900 CETZ1 FROM HALOFERAX VOLCANII - GDP BOUND MONOMER
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAIN B REPRESENTS PART OF THE C-TERMINAL TAIL OF THE SAME
REMARK 999 MOLECULE AS CHAIN A BUT HAS BEEN MAPPED SEPARATELY AS IT CANNOT
REMARK 999 CLEARLY DETERMINED WHERE IT ORIGINATES FROM.
DBREF 4B45 A 1 349 UNP D4GTC1 D4GTC1_HALVD 1 349
DBREF 4B45 B 350 360 UNP D4GTC1 D4GTC1_HALVD 350 360
SEQADV 4B45 GLY B 361 UNP D4GTC1 EXPRESSION TAG
SEQADV 4B45 SER B 362 UNP D4GTC1 EXPRESSION TAG
SEQADV 4B45 HIS B 363 UNP D4GTC1 EXPRESSION TAG
SEQADV 4B45 HIS B 364 UNP D4GTC1 EXPRESSION TAG
SEQADV 4B45 HIS B 365 UNP D4GTC1 EXPRESSION TAG
SEQADV 4B45 HIS B 366 UNP D4GTC1 EXPRESSION TAG
SEQADV 4B45 HIS B 367 UNP D4GTC1 EXPRESSION TAG
SEQADV 4B45 HIS B 368 UNP D4GTC1 EXPRESSION TAG
SEQRES 1 A 349 MET LYS THR VAL LEU ILE GLY VAL GLY GLN ALA GLY GLY
SEQRES 2 A 349 LYS LEU ALA SER ALA LEU GLN SER PHE ASP ARG GLN THR
SEQRES 3 A 349 GLY PHE GLY ALA VAL LEU ASP ALA VAL ALA VAL ASN THR
SEQRES 4 A 349 ALA LYS ALA ASP LEU GLN SER LEU PRO VAL GLU THR VAL
SEQRES 5 A 349 LEU ILE GLY GLN ASP ARG VAL ASN GLY HIS GLY VAL GLY
SEQRES 6 A 349 GLY ASP ASN GLU LEU GLY ALA ALA VAL MET GLU SER ASP
SEQRES 7 A 349 GLN THR GLU VAL MET SER ALA LEU ASP GLY ARG VAL THR
SEQRES 8 A 349 ALA GLU ALA GLU SER ILE PHE VAL VAL ALA GLY LEU GLY
SEQRES 9 A 349 GLY GLY SER GLY SER GLY GLY ALA PRO VAL LEU ALA LYS
SEQRES 10 A 349 ALA LEU ALA GLY VAL TYR ASP VAL PRO VAL TYR VAL LEU
SEQRES 11 A 349 GLY ILE LEU PRO GLY ALA ASP GLU GLY ALA LEU TYR GLN
SEQRES 12 A 349 VAL ASN ALA GLY ARG SER LEU LYS THR VAL ALA ARG GLU
SEQRES 13 A 349 ALA ASP ALA VAL LEU LEU VAL ASP ASN ASP ALA PHE ARG
SEQRES 14 A 349 SER ALA GLY GLU SER MET SER GLU GLY TYR ASP ALA ILE
SEQRES 15 A 349 ASN GLU ALA ILE ALA ARG ARG VAL GLY LEU LEU LEU ALA
SEQRES 16 A 349 ALA GLY GLU ALA THR GLU GLY VAL GLY GLU SER VAL VAL
SEQRES 17 A 349 ASP THR SER GLU VAL ILE ASN THR LEU ARG SER GLY GLY
SEQRES 18 A 349 ILE ALA ALA LEU GLY TYR ALA SER ALA GLU ALA SER PRO
SEQRES 19 A 349 ASN ALA GLU ASP ASN ILE ASN ALA VAL MET SER THR THR
SEQRES 20 A 349 ARG ARG ALA VAL LEU THR GLY THR SER LEU PRO ASP ALA
SEQRES 21 A 349 SER ASP ALA ASP ALA ALA LEU VAL VAL ILE ALA GLY GLU
SEQRES 22 A 349 PRO ASP THR ILE PRO ARG LYS GLY VAL GLU ARG ALA ARG
SEQRES 23 A 349 ARG TRP VAL GLU ASP GLU THR GLY SER MET GLN VAL ARG
SEQRES 24 A 349 GLY GLY ASP PHE PRO LEU GLU SER GLY ARG LEU ALA SER
SEQRES 25 A 349 LEU VAL LEU LEU GLY GLY VAL GLU ARG SER GLU ARG VAL
SEQRES 26 A 349 GLU SER PHE MET GLU ARG ALA ARG GLU ALA ILE ASP LYS
SEQRES 27 A 349 ALA GLU THR GLU PRO ARG GLU ASP PRO LYS GLY
SEQRES 1 B 19 MET TRP HIS SER ASP ASP LEU ASP ASP LEU LEU GLY SER
SEQRES 2 B 19 HIS HIS HIS HIS HIS HIS
HET GSP A1342 32
HETNAM GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
FORMUL 3 GSP C10 H16 N5 O13 P3 S
FORMUL 4 HOH *99(H2 O)
HELIX 1 1 GLY A 9 THR A 26 1 18
HELIX 2 2 ALA A 40 SER A 46 1 7
HELIX 3 3 GLY A 55 ASN A 60 1 6
HELIX 4 4 ASP A 67 LEU A 86 1 20
HELIX 5 5 GLY A 106 GLY A 121 1 16
HELIX 6 6 GLY A 139 ALA A 157 1 19
HELIX 7 7 ASP A 166 PHE A 168 5 3
HELIX 8 8 SER A 174 GLY A 197 1 24
HELIX 9 9 ASP A 209 ARG A 218 1 10
HELIX 10 10 ASN A 235 ASP A 238 5 4
HELIX 11 11 ASN A 239 THR A 253 1 15
HELIX 12 12 PRO A 274 ILE A 277 5 4
HELIX 13 13 PRO A 278 GLY A 294 1 17
HELIX 14 14 SER A 322 THR A 341 1 20
SHEET 1 AA10 GLU A 50 LEU A 53 0
SHEET 2 AA10 VAL A 31 ASN A 38 1 O ALA A 34 N GLU A 50
SHEET 3 AA10 THR A 3 VAL A 8 1 O THR A 3 N LEU A 32
SHEET 4 AA10 SER A 96 GLY A 102 1 O SER A 96 N VAL A 4
SHEET 5 AA10 VAL A 127 LEU A 133 1 O TYR A 128 N VAL A 99
SHEET 6 AA10 ALA A 159 ASP A 164 1 O ALA A 159 N VAL A 129
SHEET 7 AA10 ILE A 222 GLU A 231 1 O ALA A 223 N LEU A 162
SHEET 8 AA10 ARG A 309 VAL A 319 -1 O LEU A 310 N ALA A 230
SHEET 9 AA10 ALA A 263 GLY A 272 -1 N ASP A 264 O GLY A 317
SHEET 10 AA10 VAL A 298 PRO A 304 1 O ARG A 299 N VAL A 268
SITE 1 AC1 21 GLY A 9 GLN A 10 ALA A 11 LYS A 14
SITE 2 AC1 21 GLY A 65 GLY A 66 GLY A 105 GLY A 106
SITE 3 AC1 21 SER A 107 GLY A 108 GLU A 138 ASN A 165
SITE 4 AC1 21 TYR A 179 ILE A 182 ASN A 183 ASP A 209
SITE 5 AC1 21 GLU A 212 HOH A2003 HOH A2010 HOH A2012
SITE 6 AC1 21 HOH A2036
CRYST1 42.427 43.224 48.450 68.87 75.34 86.90 P 1 1
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 0.023570 -0.001276 -0.006115 0.00000
SCALE2 0.000000 0.023169 -0.008912 0.00000
SCALE3 0.000000 0.000000 0.022858 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
