HEADER PROTEIN TRANSPORT 26-JUN-03 1OIV
TITLE X-RAY STRUCTURE OF THE SMALL G PROTEIN RAB11A IN COMPLEX WITH GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED PROTEIN RAB-11A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-173;
COMPND 5 SYNONYM: RAB-11,24KG, YL8, RAB11A;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: DELETION MUTANT LACKING THE 43 C-TERMINAL RESIDUES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN TRANSPORT, SMALL G PROTEIN, INTRACELLULAR TRAFFICKING, GTP-
KEYWDS 2 BINDING, LIPOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PASQUALATO,F.SENIC-MATUGLIA,L.RENAULT,B.GOUD,J.SALAMERO,J.CHERFILS
REVDAT 4 13-DEC-23 1OIV 1 REMARK
REVDAT 3 24-FEB-09 1OIV 1 VERSN
REVDAT 2 18-MAR-04 1OIV 1 JRNL
REVDAT 1 08-JAN-04 1OIV 0
JRNL AUTH S.PASQUALATO,F.SENIC-MATUGLIA,L.RENAULT,B.GOUD,J.SALAMERO,
JRNL AUTH 2 J.CHERFILS
JRNL TITL THE STRUCTURAL GDP/GTP CYCLE OF RAB11 REVEALS A NOVEL
JRNL TITL 2 INTERFACE INVOLVED IN THE DYNAMICS OF RECYCLING ENDOSOMES
JRNL REF J.BIOL.CHEM. V. 279 11480 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14699104
JRNL DOI 10.1074/JBC.M310558200
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1189171.580
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 24954
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) : 0.210
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1702
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1556
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 103
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2670
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 191
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.66000
REMARK 3 B22 (A**2) : 3.31000
REMARK 3 B33 (A**2) : -3.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.910 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.100 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.640 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.260 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 66.75
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_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : EDO_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GDP_XPLOR_TOP.TXT
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : EDO_XPLOR_TOP.TXT
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES OF THE N-TERMINAL HIS6-TAG AND
REMARK 3 LINKER WERE DISORDERED AND NOT VISIBLE IN THE ELECTRON DENSITY
REMARK 3 MAP, AS WELL AS THE FIRST 5 RESIDUES OF RAB11A. ASP6 WAS
REMARK 3 MODELLED AS ALANINE BECAUSE ITS SIDE CHAIN WAS NOT VISIBLE
REMARK 4
REMARK 4 1OIV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1290012948.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26143
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1G16
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7M (NH4)2SO4,5%PEG400,8% 1,3
REMARK 280 BUTANEDIOL,0.1M TRIS-HCL PH8.0, PH 8.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.67450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.13850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.85050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.13850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.67450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.85050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THIS MAY BE RESULT OF CRYSTAL PACKING
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -18
REMARK 465 ARG A -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 GLY A -8
REMARK 465 ILE A -7
REMARK 465 PRO A -6
REMARK 465 LEU A -5
REMARK 465 PRO A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 ALA A -1
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 THR A 3
REMARK 465 ARG A 4
REMARK 465 ASP A 5
REMARK 465 MET B -18
REMARK 465 ARG B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 GLY B -8
REMARK 465 ILE B -7
REMARK 465 PRO B -6
REMARK 465 LEU B -5
REMARK 465 PRO B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 ALA B -1
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 THR B 3
REMARK 465 ARG B 4
REMARK 465 ASP B 5
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 ASP A 6 CG OD1 OD2
REMARK 470 ASP B 6 CG OD1 OD2
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 GLN A 70 -73.73 -66.21
REMARK 500 ARG A 74 -70.59 -9.21
REMARK 500 LYS A 125 33.51 74.92
REMARK 500 LEU A 128 47.16 -93.42
REMARK 500 SER A 158 -13.48 83.76
REMARK 500 ASN A 160 7.52 56.42
REMARK 500 LYS B 125 40.14 72.77
REMARK 500 SER B 158 -4.20 80.42
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 SO4 A1175
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A1174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B1175
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OIX RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE SMALL G PROTEIN RAB11A IN COMPLEX WITH GDP
REMARK 900 AND PI
REMARK 900 RELATED ID: 1OIW RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE SMALL G PROTEIN RAB11A IN COMPLEX WITH
REMARK 900 GTPGAMMAS
DBREF 1OIV A -18 -1 PDB 1OIV 1OIV -18 -1
DBREF 1OIV A 1 173 UNP P24410 R11A_HUMAN 1 173
DBREF 1OIV B -18 -1 PDB 1OIV 1OIV -18 -1
DBREF 1OIV B 1 173 UNP P24410 R11A_HUMAN 1 173
SEQRES 1 A 191 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY ILE PRO
SEQRES 2 A 191 LEU PRO GLY ARG ALA MET GLY THR ARG ASP ASP GLU TYR
SEQRES 3 A 191 ASP TYR LEU PHE LYS VAL VAL LEU ILE GLY ASP SER GLY
SEQRES 4 A 191 VAL GLY LYS SER ASN LEU LEU SER ARG PHE THR ARG ASN
SEQRES 5 A 191 GLU PHE ASN LEU GLU SER LYS SER THR ILE GLY VAL GLU
SEQRES 6 A 191 PHE ALA THR ARG SER ILE GLN VAL ASP GLY LYS THR ILE
SEQRES 7 A 191 LYS ALA GLN ILE TRP ASP THR ALA GLY GLN GLU ARG TYR
SEQRES 8 A 191 ARG ALA ILE THR SER ALA TYR TYR ARG GLY ALA VAL GLY
SEQRES 9 A 191 ALA LEU LEU VAL TYR ASP ILE ALA LYS HIS LEU THR TYR
SEQRES 10 A 191 GLU ASN VAL GLU ARG TRP LEU LYS GLU LEU ARG ASP HIS
SEQRES 11 A 191 ALA ASP SER ASN ILE VAL ILE MET LEU VAL GLY ASN LYS
SEQRES 12 A 191 SER ASP LEU ARG HIS LEU ARG ALA VAL PRO THR ASP GLU
SEQRES 13 A 191 ALA ARG ALA PHE ALA GLU LYS ASN GLY LEU SER PHE ILE
SEQRES 14 A 191 GLU THR SER ALA LEU ASP SER THR ASN VAL GLU ALA ALA
SEQRES 15 A 191 PHE GLN THR ILE LEU THR GLU ILE TYR
SEQRES 1 B 191 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY ILE PRO
SEQRES 2 B 191 LEU PRO GLY ARG ALA MET GLY THR ARG ASP ASP GLU TYR
SEQRES 3 B 191 ASP TYR LEU PHE LYS VAL VAL LEU ILE GLY ASP SER GLY
SEQRES 4 B 191 VAL GLY LYS SER ASN LEU LEU SER ARG PHE THR ARG ASN
SEQRES 5 B 191 GLU PHE ASN LEU GLU SER LYS SER THR ILE GLY VAL GLU
SEQRES 6 B 191 PHE ALA THR ARG SER ILE GLN VAL ASP GLY LYS THR ILE
SEQRES 7 B 191 LYS ALA GLN ILE TRP ASP THR ALA GLY GLN GLU ARG TYR
SEQRES 8 B 191 ARG ALA ILE THR SER ALA TYR TYR ARG GLY ALA VAL GLY
SEQRES 9 B 191 ALA LEU LEU VAL TYR ASP ILE ALA LYS HIS LEU THR TYR
SEQRES 10 B 191 GLU ASN VAL GLU ARG TRP LEU LYS GLU LEU ARG ASP HIS
SEQRES 11 B 191 ALA ASP SER ASN ILE VAL ILE MET LEU VAL GLY ASN LYS
SEQRES 12 B 191 SER ASP LEU ARG HIS LEU ARG ALA VAL PRO THR ASP GLU
SEQRES 13 B 191 ALA ARG ALA PHE ALA GLU LYS ASN GLY LEU SER PHE ILE
SEQRES 14 B 191 GLU THR SER ALA LEU ASP SER THR ASN VAL GLU ALA ALA
SEQRES 15 B 191 PHE GLN THR ILE LEU THR GLU ILE TYR
HET GDP A1174 28
HET SO4 A1175 5
HET EDO B1174 4
HET GDP B1175 28
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 EDO C2 H6 O2
FORMUL 7 HOH *191(H2 O)
HELIX 1 1 GLY A 23 ASN A 34 1 12
HELIX 2 2 TYR A 73 ARG A 82 1 10
HELIX 3 3 LYS A 95 ASN A 101 1 7
HELIX 4 4 ASN A 101 ALA A 113 1 13
HELIX 5 5 LEU A 128 ARG A 132 5 5
HELIX 6 6 PRO A 135 GLY A 147 1 13
HELIX 7 7 ASN A 160 TYR A 173 1 14
HELIX 8 8 GLY B 23 ASN B 34 1 12
HELIX 9 9 TYR B 73 ARG B 82 1 10
HELIX 10 10 LYS B 95 ASN B 101 1 7
HELIX 11 11 ASN B 101 ALA B 113 1 13
HELIX 12 12 LYS B 125 ARG B 132 5 8
HELIX 13 13 PRO B 135 ASN B 146 1 12
HELIX 14 14 ASN B 160 TYR B 173 1 14
SHEET 1 AA12 SER A 149 GLU A 152 0
SHEET 2 AA12 VAL A 118 ASN A 124 1 O ILE A 119 N SER A 149
SHEET 3 AA12 ALA A 84 ASP A 92 1 O VAL A 85 N VAL A 118
SHEET 4 AA12 TYR A 10 ILE A 17 1 O LYS A 13 N VAL A 85
SHEET 5 AA12 LYS A 58 THR A 67 1 O LYS A 61 N PHE A 12
SHEET 6 AA12 VAL A 46 VAL A 55 -1 O GLU A 47 N ASP A 66
SHEET 7 AA12 VAL B 46 VAL B 55 -1 O VAL B 46 N PHE A 48
SHEET 8 AA12 LYS B 58 THR B 67 -1 O LYS B 58 N VAL B 55
SHEET 9 AA12 TYR B 10 ILE B 17 1 O TYR B 10 N LYS B 61
SHEET 10 AA12 GLY B 86 ASP B 92 1 O GLY B 86 N VAL B 15
SHEET 11 AA12 VAL B 118 ASN B 124 1 O VAL B 118 N ALA B 87
SHEET 12 AA12 SER B 149 GLU B 152 1 O SER B 149 N LEU B 121
SITE 1 AC1 4 HOH A2084 ARG B 129 ARG B 132 HOH B2086
SITE 1 AC2 21 SER A 20 GLY A 21 VAL A 22 GLY A 23
SITE 2 AC2 21 LYS A 24 SER A 25 ASN A 26 PHE A 36
SITE 3 AC2 21 ASN A 37 LEU A 38 SER A 40 ASN A 124
SITE 4 AC2 21 LYS A 125 ASP A 127 LEU A 128 SER A 154
SITE 5 AC2 21 ALA A 155 LEU A 156 HOH A2080 HOH A2081
SITE 6 AC2 21 HOH A2083
SITE 1 AC3 6 ASN A 116 TYR B 99 GLU B 100 VAL B 102
SITE 2 AC3 6 GLU B 103 HOH B2064
SITE 1 AC4 25 GLU A 162 HOH A2037 ASP B 19 SER B 20
SITE 2 AC4 25 GLY B 21 VAL B 22 GLY B 23 LYS B 24
SITE 3 AC4 25 SER B 25 ASN B 26 PHE B 36 ASN B 37
SITE 4 AC4 25 LEU B 38 SER B 40 SER B 42 ASN B 124
SITE 5 AC4 25 LYS B 125 ASP B 127 LEU B 128 SER B 154
SITE 6 AC4 25 ALA B 155 LEU B 156 HOH B2105 HOH B2106
SITE 7 AC4 25 HOH B2107
CRYST1 47.349 69.701 108.277 90.00 90.00 90.00 P 21 21 21 8
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 0.021120 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009235 0.00000
MTRIX1 1 -0.317740 -0.900020 0.298330 2.64872 1
MTRIX2 1 -0.896050 0.182130 -0.404870 5.48818 1
MTRIX3 1 0.310050 -0.395960 -0.864340 10.76037 1
(ATOM LINES ARE NOT SHOWN.)
END