HEADER TRANSPORT PROTEIN 21-JUN-06 2HEI
TITLE CRYSTAL STRUCTURE OF HUMAN RAB5B IN COMPLEX WITH GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED PROTEIN RAB-5B;
COMPND 3 CHAIN: A, B;
COMPND 4 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: RAB5B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE-3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC
KEYWDS G-PROTEIN, RAB, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 2 SGC, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.HONG,L.SHEN,J.WANG,W.TEMPEL,R.LANDRY,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 M.SUNDSTROM,J.WEIGELT,A.BOCHKAREV,H.PARK,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 4 30-AUG-23 2HEI 1 REMARK SEQADV
REVDAT 3 18-OCT-17 2HEI 1 REMARK
REVDAT 2 24-FEB-09 2HEI 1 VERSN
REVDAT 1 04-JUL-06 2HEI 0
JRNL AUTH B.HONG,L.SHEN,J.WANG,W.TEMPEL,R.LANDRY,C.H.ARROWSMITH,
JRNL AUTH 2 A.M.EDWARDS,M.SUNDSTROM,J.WEIGELT,A.BOCHKAREV,H.PARK
JRNL TITL CRYSTAL STRUCTURE OF HUMAN RAB5B IN COMPLEX WITH GDP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 45443
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.262
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.327
REMARK 3 FREE R VALUE TEST SET COUNT : 2875
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3331
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2559
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37500
REMARK 3 B22 (A**2) : 0.51700
REMARK 3 B33 (A**2) : -0.14300
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): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.000
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2690 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1770 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3649 ; 1.488 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4336 ; 1.139 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 328 ; 6.085 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 112 ;34.633 ;24.821
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 463 ;12.151 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;14.429 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 421 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2910 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 536 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 498 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1876 ; 0.194 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1282 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1307 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 128 ; 0.131 ; 0.200
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): 26 ; 0.229 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.269 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.106 ; 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): 1809 ; 2.432 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 664 ; 0.687 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2615 ; 2.907 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1205 ; 2.466 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1032 ; 3.232 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; 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 BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2HEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50161
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.67900
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1N6I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% P3350, 0.1M NAOAC, PH 4.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 20.65100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.75050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.18500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.75050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.65100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.18500
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). ACCORDING TO AUTHORS, THE
REMARK 300 BIOLOGICAL UNIT OF THE PROTEIN IS NOT KNOWN
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, 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 GLY A 13
REMARK 465 SER A 14
REMARK 465 ALA A 15
REMARK 465 SER A 16
REMARK 465 LYS A 17
REMARK 465 ASP A 65
REMARK 465 ASP A 66
REMARK 465 THR A 67
REMARK 465 SER A 184
REMARK 465 GLU A 185
REMARK 465 PRO A 186
REMARK 465 GLN A 187
REMARK 465 ASN A 188
REMARK 465 LEU A 189
REMARK 465 GLY A 190
REMARK 465 GLY A 191
REMARK 465 GLY B 13
REMARK 465 SER B 14
REMARK 465 ALA B 15
REMARK 465 SER B 16
REMARK 465 ASP B 65
REMARK 465 ASP B 66
REMARK 465 SER B 184
REMARK 465 GLU B 185
REMARK 465 PRO B 186
REMARK 465 GLN B 187
REMARK 465 ASN B 188
REMARK 465 LEU B 189
REMARK 465 GLY B 190
REMARK 465 GLY B 191
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 ARG A 91 CZ NH1 NH2
REMARK 470 GLN A 105 CD OE1 NE2
REMARK 470 LYS A 180 CE NZ
REMARK 470 LYS B 17 CG CD CE NZ
REMARK 470 GLN B 105 CD OE1 NE2
REMARK 470 ARG B 120 NE CZ NH1 NH2
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 30 7.58 83.25
REMARK 500 ALA A 167 -3.83 82.36
REMARK 500 ALA B 30 8.90 80.00
REMARK 500 LEU B 137 47.99 -98.05
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1D A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1D B 302
DBREF 2HEI A 15 191 UNP P61020 RAB5B_HUMAN 15 191
DBREF 2HEI B 15 191 UNP P61020 RAB5B_HUMAN 15 191
SEQADV 2HEI GLY A 13 UNP P61020 CLONING ARTIFACT
SEQADV 2HEI SER A 14 UNP P61020 CLONING ARTIFACT
SEQADV 2HEI GLY B 13 UNP P61020 CLONING ARTIFACT
SEQADV 2HEI SER B 14 UNP P61020 CLONING ARTIFACT
SEQRES 1 A 179 GLY SER ALA SER LYS ILE CYS GLN PHE LYS LEU VAL LEU
SEQRES 2 A 179 LEU GLY GLU SER ALA VAL GLY LYS SER SER LEU VAL LEU
SEQRES 3 A 179 ARG PHE VAL LYS GLY GLN PHE HIS GLU TYR GLN GLU SER
SEQRES 4 A 179 THR ILE GLY ALA ALA PHE LEU THR GLN SER VAL CYS LEU
SEQRES 5 A 179 ASP ASP THR THR VAL LYS PHE GLU ILE TRP ASP THR ALA
SEQRES 6 A 179 GLY GLN GLU ARG TYR HIS SER LEU ALA PRO MET TYR TYR
SEQRES 7 A 179 ARG GLY ALA GLN ALA ALA ILE VAL VAL TYR ASP ILE THR
SEQRES 8 A 179 ASN GLN GLU THR PHE ALA ARG ALA LYS THR TRP VAL LYS
SEQRES 9 A 179 GLU LEU GLN ARG GLN ALA SER PRO SER ILE VAL ILE ALA
SEQRES 10 A 179 LEU ALA GLY ASN LYS ALA ASP LEU ALA ASN LYS ARG MET
SEQRES 11 A 179 VAL GLU TYR GLU GLU ALA GLN ALA TYR ALA ASP ASP ASN
SEQRES 12 A 179 SER LEU LEU PHE MET GLU THR SER ALA LYS THR ALA MET
SEQRES 13 A 179 ASN VAL ASN ASP LEU PHE LEU ALA ILE ALA LYS LYS LEU
SEQRES 14 A 179 PRO LYS SER GLU PRO GLN ASN LEU GLY GLY
SEQRES 1 B 179 GLY SER ALA SER LYS ILE CYS GLN PHE LYS LEU VAL LEU
SEQRES 2 B 179 LEU GLY GLU SER ALA VAL GLY LYS SER SER LEU VAL LEU
SEQRES 3 B 179 ARG PHE VAL LYS GLY GLN PHE HIS GLU TYR GLN GLU SER
SEQRES 4 B 179 THR ILE GLY ALA ALA PHE LEU THR GLN SER VAL CYS LEU
SEQRES 5 B 179 ASP ASP THR THR VAL LYS PHE GLU ILE TRP ASP THR ALA
SEQRES 6 B 179 GLY GLN GLU ARG TYR HIS SER LEU ALA PRO MET TYR TYR
SEQRES 7 B 179 ARG GLY ALA GLN ALA ALA ILE VAL VAL TYR ASP ILE THR
SEQRES 8 B 179 ASN GLN GLU THR PHE ALA ARG ALA LYS THR TRP VAL LYS
SEQRES 9 B 179 GLU LEU GLN ARG GLN ALA SER PRO SER ILE VAL ILE ALA
SEQRES 10 B 179 LEU ALA GLY ASN LYS ALA ASP LEU ALA ASN LYS ARG MET
SEQRES 11 B 179 VAL GLU TYR GLU GLU ALA GLN ALA TYR ALA ASP ASP ASN
SEQRES 12 B 179 SER LEU LEU PHE MET GLU THR SER ALA LYS THR ALA MET
SEQRES 13 B 179 ASN VAL ASN ASP LEU PHE LEU ALA ILE ALA LYS LYS LEU
SEQRES 14 B 179 PRO LYS SER GLU PRO GLN ASN LEU GLY GLY
HET GDP A 201 28
HET D1D A 202 8
HET GDP B 301 28
HET D1D B 302 8
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM D1D (4S,5S)-1,2-DITHIANE-4,5-DIOL
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 4 D1D 2(C4 H8 O2 S2)
FORMUL 7 HOH *124(H2 O)
HELIX 1 1 GLY A 32 GLY A 43 1 12
HELIX 2 2 TYR A 82 SER A 84 5 3
HELIX 3 3 LEU A 85 ARG A 91 1 7
HELIX 4 4 ASN A 104 ALA A 122 1 19
HELIX 5 5 LYS A 134 ARG A 141 5 8
HELIX 6 6 GLU A 144 ASN A 155 1 12
HELIX 7 7 ASN A 169 LEU A 181 1 13
HELIX 8 8 GLY B 32 GLY B 43 1 12
HELIX 9 9 TYR B 82 SER B 84 5 3
HELIX 10 10 LEU B 85 ARG B 91 1 7
HELIX 11 11 ASN B 104 ALA B 122 1 19
HELIX 12 12 LYS B 134 ARG B 141 5 8
HELIX 13 13 GLU B 144 ASN B 155 1 12
HELIX 14 14 ASN B 169 LEU B 181 1 13
SHEET 1 A 6 LEU A 58 VAL A 62 0
SHEET 2 A 6 VAL A 69 TRP A 74 -1 O ILE A 73 N LEU A 58
SHEET 3 A 6 CYS A 19 LEU A 26 1 N CYS A 19 O LYS A 70
SHEET 4 A 6 ALA A 95 ASP A 101 1 O ILE A 97 N LEU A 26
SHEET 5 A 6 VAL A 127 ASN A 133 1 O ALA A 129 N VAL A 98
SHEET 6 A 6 LEU A 158 GLU A 161 1 O LEU A 158 N LEU A 130
SHEET 1 B 6 LEU B 58 VAL B 62 0
SHEET 2 B 6 THR B 68 ASP B 75 -1 O VAL B 69 N VAL B 62
SHEET 3 B 6 ILE B 18 LEU B 26 1 N PHE B 21 O LYS B 70
SHEET 4 B 6 ALA B 95 ASP B 101 1 O VAL B 99 N LEU B 26
SHEET 5 B 6 VAL B 127 ASN B 133 1 O ASN B 133 N TYR B 100
SHEET 6 B 6 LEU B 158 GLU B 161 1 O LEU B 158 N LEU B 130
SITE 1 AC1 22 ALA A 30 VAL A 31 GLY A 32 LYS A 33
SITE 2 AC1 22 SER A 34 SER A 35 PHE A 45 GLU A 47
SITE 3 AC1 22 TYR A 48 SER A 51 ALA A 77 ASN A 133
SITE 4 AC1 22 LYS A 134 ASP A 136 LEU A 137 SER A 163
SITE 5 AC1 22 ALA A 164 LYS A 165 HOH A 221 HOH A 223
SITE 6 AC1 22 HOH A 244 HOH A 266
SITE 1 AC2 9 THR A 76 GLN A 79 GLU A 80 HIS A 83
SITE 2 AC2 9 ALA A 86 TYR A 89 TYR A 90 TRP A 114
SITE 3 AC2 9 GLU A 117
SITE 1 AC3 23 ALA B 30 VAL B 31 GLY B 32 LYS B 33
SITE 2 AC3 23 SER B 34 SER B 35 PHE B 45 GLU B 47
SITE 3 AC3 23 TYR B 48 SER B 51 ALA B 77 ASN B 133
SITE 4 AC3 23 LYS B 134 ASP B 136 LEU B 137 SER B 163
SITE 5 AC3 23 ALA B 164 LYS B 165 HOH B 310 HOH B 315
SITE 6 AC3 23 HOH B 338 HOH B 360 HOH B 361
SITE 1 AC4 8 THR B 76 GLN B 79 GLU B 80 HIS B 83
SITE 2 AC4 8 ALA B 86 TYR B 89 TRP B 114 GLU B 117
CRYST1 41.302 78.370 95.501 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 0.024212 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012760 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010471 0.00000
(ATOM LINES ARE NOT SHOWN.)
END