HEADER TRANSPORT PROTEIN 08-APR-15 4UJ5
TITLE CRYSTAL STRUCTURE OF HUMAN RAB11-RABIN8-FIP3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED PROTEIN RAB-11A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: GTPASE DOMAIN, RESIDUES 6-186;
COMPND 5 SYNONYM: RAB-11, YL8, RAB-11, YL8, RAB11A;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RAB-3A-INTERACTING PROTEIN;
COMPND 10 CHAIN: C, D;
COMPND 11 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 286-476;
COMPND 12 SYNONYM: RAB3A-INTERACTING PROTEIN, RABIN-3, SSX2-INTERACTING
COMPND 13 PROTEIN, RAB3A-INTERACTING PROTEIN, RABIN-3, SSX2-INTERACTING
COMPND 14 PROTEIN, RABIN8;
COMPND 15 ENGINEERED: YES
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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS TRANSPORT PROTEIN, CILIARY TARGETING COMPLEX, CILIUM, VESICU
KEYWDS 2 TRANSPORT, MEMBRANE TRAFFICKING, RABIN8, RAB11, FIP3
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VETTER,E.LORENTZEN
REVDAT 4 10-JAN-24 4UJ5 1 REMARK LINK
REVDAT 3 16-SEP-15 4UJ5 1 JRNL
REVDAT 2 19-AUG-15 4UJ5 1 JRNL
REVDAT 1 12-AUG-15 4UJ5 0
JRNL AUTH M.VETTER,R.STEHLE,C.BASQUIN,E.LORENTZEN
JRNL TITL STRUCTURE OF RAB11-FIP3-RABIN8 REVEALS SIMULTANEOUS BINDING
JRNL TITL 2 OF FIP3 AND RABIN8 EFFECTORS TO RAB11.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 22 695 2015
JRNL REFN ISSN 1545-9993
JRNL PMID 26258637
JRNL DOI 10.1038/NSMB.3065
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.930
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 3 NUMBER OF REFLECTIONS : 24374
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2270
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 43.6481 - 6.5535 0.91 2639 138 0.1666 0.1968
REMARK 3 2 6.5535 - 5.2045 0.94 2729 149 0.2085 0.2587
REMARK 3 3 5.2045 - 4.5474 0.92 2672 139 0.1803 0.2435
REMARK 3 4 4.5474 - 4.1320 0.91 2651 129 0.1743 0.2617
REMARK 3 5 4.1320 - 3.8360 0.90 2646 144 0.2008 0.2723
REMARK 3 6 3.8360 - 3.6099 0.93 2689 143 0.2006 0.2566
REMARK 3 7 3.6099 - 3.4292 0.94 2734 144 0.2151 0.2782
REMARK 3 8 3.4292 - 3.2800 0.95 2761 147 0.2380 0.3041
REMARK 3 9 3.2800 - 3.1538 0.95 2766 148 0.2355 0.2774
REMARK 3 10 3.1538 - 3.0450 0.96 2798 148 0.2596 0.3069
REMARK 3 11 3.0450 - 2.9498 0.93 2749 146 0.2973 0.3707
REMARK 3 12 2.9498 - 2.8655 0.90 2579 135 0.3328 0.4233
REMARK 3 13 2.8655 - 2.7901 0.89 2628 137 0.3499 0.3601
REMARK 3 14 2.7901 - 2.7220 0.91 2591 140 0.3668 0.4329
REMARK 3 15 2.7220 - 2.6601 0.92 2718 146 0.3693 0.3995
REMARK 3 16 2.6601 - 2.6035 0.88 2551 137 0.3887 0.4126
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.60
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 : 0.005 5302
REMARK 3 ANGLE : 1.072 7223
REMARK 3 CHIRALITY : 0.039 830
REMARK 3 PLANARITY : 0.004 915
REMARK 3 DIHEDRAL : 14.065 1857
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : NULL
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4UJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24951
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.530
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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 1YZK
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0, 0.2M LITHIUM
REMARK 280 SULFATE AND 24% PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 54.10100
REMARK 290 SMTRY3 2 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 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 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.4 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.3 KCAL/MOL
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 GLY A 2
REMARK 465 ALA A 3
REMARK 465 GLU A 71
REMARK 465 ARG A 72
REMARK 465 TYR A 73
REMARK 465 GLN A 180
REMARK 465 MET A 181
REMARK 465 SER A 182
REMARK 465 ASP A 183
REMARK 465 ARG A 184
REMARK 465 ARG A 185
REMARK 465 GLU A 186
REMARK 465 GLY B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 SER B 5
REMARK 465 ASP B 6
REMARK 465 LYS B 179
REMARK 465 GLN B 180
REMARK 465 MET B 181
REMARK 465 SER B 182
REMARK 465 ASP B 183
REMARK 465 ARG B 184
REMARK 465 ARG B 185
REMARK 465 GLU B 186
REMARK 465 GLY C 266
REMARK 465 ALA C 267
REMARK 465 ALA C 268
REMARK 465 SER C 269
REMARK 465 ASN C 270
REMARK 465 LYS C 271
REMARK 465 SER C 272
REMARK 465 THR C 273
REMARK 465 SER C 274
REMARK 465 SER C 275
REMARK 465 ALA C 276
REMARK 465 MET C 277
REMARK 465 SER C 278
REMARK 465 GLY C 279
REMARK 465 SER C 280
REMARK 465 HIS C 281
REMARK 465 GLN C 282
REMARK 465 ASP C 283
REMARK 465 LEU C 284
REMARK 465 SER C 285
REMARK 465 VAL C 286
REMARK 465 ILE C 287
REMARK 465 SER C 369
REMARK 465 ALA C 370
REMARK 465 VAL C 371
REMARK 465 LEU C 460
REMARK 465 GLY D 266
REMARK 465 ALA D 267
REMARK 465 ALA D 268
REMARK 465 SER D 269
REMARK 465 ASN D 270
REMARK 465 LYS D 271
REMARK 465 SER D 272
REMARK 465 THR D 273
REMARK 465 SER D 274
REMARK 465 SER D 275
REMARK 465 ALA D 276
REMARK 465 MET D 277
REMARK 465 SER D 278
REMARK 465 GLY D 279
REMARK 465 SER D 280
REMARK 465 HIS D 281
REMARK 465 GLN D 282
REMARK 465 ASP D 283
REMARK 465 LEU D 284
REMARK 465 SER D 285
REMARK 465 LEU D 360
REMARK 465 GLN D 361
REMARK 465 PRO D 362
REMARK 465 ILE D 363
REMARK 465 ARG D 364
REMARK 465 PHE D 365
REMARK 465 VAL D 366
REMARK 465 LYS D 367
REMARK 465 ALA D 368
REMARK 465 SER D 369
REMARK 465 ALA D 370
REMARK 465 VAL D 371
REMARK 465 GLU D 372
REMARK 465 CYS D 373
REMARK 465 GLY D 374
REMARK 465 GLY D 375
REMARK 465 PRO D 376
REMARK 465 LYS D 377
REMARK 465 LYS D 378
REMARK 465 CYS D 379
REMARK 465 ALA D 380
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 GLU A 7 CG CD OE1 OE2
REMARK 470 TYR A 10 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 33 NE CZ NH1 NH2
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 ASP A 56 CG OD1 OD2
REMARK 470 LYS A 58 CG CD CE NZ
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 SER A 78 OG
REMARK 470 ARG A 82 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 103 CG CD OE1 OE2
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 TYR A 173 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 174 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 176 CG1 CG2
REMARK 470 GLN A 178 CG CD OE1 NE2
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 GLU B 7 CG CD OE1 OE2
REMARK 470 TYR B 10 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 41 CG CD CE NZ
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 LEU B 70 CG CD1 CD2
REMARK 470 GLU B 71 CG CD OE1 OE2
REMARK 470 ARG B 72 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 82 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 95 CG CD CE NZ
REMARK 470 GLU B 103 CG CD OE1 OE2
REMARK 470 ARG B 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 107 CG CD CE NZ
REMARK 470 ARG B 110 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 SER B 158 OG
REMARK 470 ILE B 175 CG1 CG2 CD1
REMARK 470 SER B 177 OG
REMARK 470 GLN B 178 CG CD OE1 NE2
REMARK 470 GLN C 288 CG CD OE1 NE2
REMARK 470 ILE C 290 CG1 CG2 CD1
REMARK 470 VAL C 291 CG1 CG2
REMARK 470 LYS C 292 CG CD CE NZ
REMARK 470 LYS C 337 CG CD CE NZ
REMARK 470 ILE C 363 CG1 CG2 CD1
REMARK 470 ARG C 364 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 365 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 367 CG CD CE NZ
REMARK 470 LYS C 386 CG CD CE NZ
REMARK 470 LYS C 389 CG CD CE NZ
REMARK 470 LYS C 430 CG CD CE NZ
REMARK 470 GLN C 431 CG CD OE1 NE2
REMARK 470 LYS C 457 CG CD CE NZ
REMARK 470 GLU C 459 CG CD OE1 OE2
REMARK 470 GLN D 288 CG CD OE1 NE2
REMARK 470 ILE D 290 CG1 CG2 CD1
REMARK 470 VAL D 291 CG1 CG2
REMARK 470 LYS D 292 CG CD CE NZ
REMARK 470 ARG D 306 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 337 CG CD CE NZ
REMARK 470 GLU D 346 CG CD OE1 OE2
REMARK 470 LEU D 381 CG CD1 CD2
REMARK 470 GLN D 384 CG CD OE1 NE2
REMARK 470 SER D 385 OG
REMARK 470 LYS D 386 CG CD CE NZ
REMARK 470 SER D 387 OG
REMARK 470 ARG D 391 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 393 CG CD CE NZ
REMARK 470 ASP D 396 CG OD1 OD2
REMARK 470 SER D 397 OG
REMARK 470 LYS D 430 CG CD CE NZ
REMARK 470 GLN D 431 CG CD OE1 NE2
REMARK 470 GLU D 458 CG CD OE1 OE2
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 SER A 158 -4.31 74.68
REMARK 500 ASP B 9 -60.37 -109.39
REMARK 500 GLU B 71 41.92 -100.35
REMARK 500 SER B 158 -1.99 74.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D2005 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH D2006 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH D2030 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH D2031 DISTANCE = 8.17 ANGSTROMS
REMARK 525 HOH D2032 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH D2033 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH D2034 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH D2035 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH D2036 DISTANCE = 7.52 ANGSTROMS
REMARK 525 HOH D2037 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH D2038 DISTANCE = 6.45 ANGSTROMS
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 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 25 OG
REMARK 620 2 THR A 43 OG1 86.8
REMARK 620 3 GNP A 201 O3G 169.4 94.1
REMARK 620 4 GNP A 201 O2B 93.4 173.5 86.9
REMARK 620 5 HOH A2006 O 91.7 98.9 98.6 74.6
REMARK 620 6 HOH A2007 O 83.4 93.3 86.0 93.2 166.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 25 OG
REMARK 620 2 THR B 43 OG1 77.6
REMARK 620 3 GNP B 201 O2B 93.8 155.1
REMARK 620 4 GNP B 201 O3G 154.3 82.4 97.7
REMARK 620 5 HOH B2006 O 73.2 81.3 73.9 88.1
REMARK 620 6 HOH B2007 O 119.3 87.6 116.7 75.3 161.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UJ3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN RAB11-RABIN8-FIP3
REMARK 900 RELATED ID: 4UJ4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN RAB11-RABIN8-FIP3
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 Q70L POINT MUTATION
DBREF 4UJ5 A 6 186 UNP P62491 RB11A_HUMAN 6 186
DBREF 4UJ5 B 6 186 UNP P62491 RB11A_HUMAN 6 186
DBREF 4UJ5 C 270 460 UNP Q96QF0 RAB3I_HUMAN 286 476
DBREF 4UJ5 D 270 460 UNP Q96QF0 RAB3I_HUMAN 286 476
SEQADV 4UJ5 GLY A 2 UNP P62491 EXPRESSION TAG
SEQADV 4UJ5 ALA A 3 UNP P62491 EXPRESSION TAG
SEQADV 4UJ5 ALA A 4 UNP P62491 EXPRESSION TAG
SEQADV 4UJ5 SER A 5 UNP P62491 EXPRESSION TAG
SEQADV 4UJ5 LEU A 70 UNP P62491 GLN 70 ENGINEERED MUTATION
SEQADV 4UJ5 GLY B 2 UNP P62491 EXPRESSION TAG
SEQADV 4UJ5 ALA B 3 UNP P62491 EXPRESSION TAG
SEQADV 4UJ5 ALA B 4 UNP P62491 EXPRESSION TAG
SEQADV 4UJ5 SER B 5 UNP P62491 EXPRESSION TAG
SEQADV 4UJ5 LEU B 70 UNP P62491 GLN 70 ENGINEERED MUTATION
SEQADV 4UJ5 GLY C 266 UNP Q96QF0 EXPRESSION TAG
SEQADV 4UJ5 ALA C 267 UNP Q96QF0 EXPRESSION TAG
SEQADV 4UJ5 ALA C 268 UNP Q96QF0 EXPRESSION TAG
SEQADV 4UJ5 SER C 269 UNP Q96QF0 EXPRESSION TAG
SEQADV 4UJ5 GLY D 266 UNP Q96QF0 EXPRESSION TAG
SEQADV 4UJ5 ALA D 267 UNP Q96QF0 EXPRESSION TAG
SEQADV 4UJ5 ALA D 268 UNP Q96QF0 EXPRESSION TAG
SEQADV 4UJ5 SER D 269 UNP Q96QF0 EXPRESSION TAG
SEQRES 1 A 185 GLY ALA ALA SER ASP GLU TYR ASP TYR LEU PHE LYS VAL
SEQRES 2 A 185 VAL LEU ILE GLY ASP SER GLY VAL GLY LYS SER ASN LEU
SEQRES 3 A 185 LEU SER ARG PHE THR ARG ASN GLU PHE ASN LEU GLU SER
SEQRES 4 A 185 LYS SER THR ILE GLY VAL GLU PHE ALA THR ARG SER ILE
SEQRES 5 A 185 GLN VAL ASP GLY LYS THR ILE LYS ALA GLN ILE TRP ASP
SEQRES 6 A 185 THR ALA GLY LEU GLU ARG TYR ARG ALA ILE THR SER ALA
SEQRES 7 A 185 TYR TYR ARG GLY ALA VAL GLY ALA LEU LEU VAL TYR ASP
SEQRES 8 A 185 ILE ALA LYS HIS LEU THR TYR GLU ASN VAL GLU ARG TRP
SEQRES 9 A 185 LEU LYS GLU LEU ARG ASP HIS ALA ASP SER ASN ILE VAL
SEQRES 10 A 185 ILE MET LEU VAL GLY ASN LYS SER ASP LEU ARG HIS LEU
SEQRES 11 A 185 ARG ALA VAL PRO THR ASP GLU ALA ARG ALA PHE ALA GLU
SEQRES 12 A 185 LYS ASN GLY LEU SER PHE ILE GLU THR SER ALA LEU ASP
SEQRES 13 A 185 SER THR ASN VAL GLU ALA ALA PHE GLN THR ILE LEU THR
SEQRES 14 A 185 GLU ILE TYR ARG ILE VAL SER GLN LYS GLN MET SER ASP
SEQRES 15 A 185 ARG ARG GLU
SEQRES 1 B 185 GLY ALA ALA SER ASP GLU TYR ASP TYR LEU PHE LYS VAL
SEQRES 2 B 185 VAL LEU ILE GLY ASP SER GLY VAL GLY LYS SER ASN LEU
SEQRES 3 B 185 LEU SER ARG PHE THR ARG ASN GLU PHE ASN LEU GLU SER
SEQRES 4 B 185 LYS SER THR ILE GLY VAL GLU PHE ALA THR ARG SER ILE
SEQRES 5 B 185 GLN VAL ASP GLY LYS THR ILE LYS ALA GLN ILE TRP ASP
SEQRES 6 B 185 THR ALA GLY LEU GLU ARG TYR ARG ALA ILE THR SER ALA
SEQRES 7 B 185 TYR TYR ARG GLY ALA VAL GLY ALA LEU LEU VAL TYR ASP
SEQRES 8 B 185 ILE ALA LYS HIS LEU THR TYR GLU ASN VAL GLU ARG TRP
SEQRES 9 B 185 LEU LYS GLU LEU ARG ASP HIS ALA ASP SER ASN ILE VAL
SEQRES 10 B 185 ILE MET LEU VAL GLY ASN LYS SER ASP LEU ARG HIS LEU
SEQRES 11 B 185 ARG ALA VAL PRO THR ASP GLU ALA ARG ALA PHE ALA GLU
SEQRES 12 B 185 LYS ASN GLY LEU SER PHE ILE GLU THR SER ALA LEU ASP
SEQRES 13 B 185 SER THR ASN VAL GLU ALA ALA PHE GLN THR ILE LEU THR
SEQRES 14 B 185 GLU ILE TYR ARG ILE VAL SER GLN LYS GLN MET SER ASP
SEQRES 15 B 185 ARG ARG GLU
SEQRES 1 C 195 GLY ALA ALA SER ASN LYS SER THR SER SER ALA MET SER
SEQRES 2 C 195 GLY SER HIS GLN ASP LEU SER VAL ILE GLN PRO ILE VAL
SEQRES 3 C 195 LYS ASP CYS LYS GLU ALA ASP LEU SER LEU TYR ASN GLU
SEQRES 4 C 195 PHE ARG LEU TRP LYS ASP GLU PRO THR MET ASP ARG THR
SEQRES 5 C 195 CYS PRO PHE LEU ASP LYS ILE TYR GLN GLU ASP ILE PHE
SEQRES 6 C 195 PRO CYS LEU THR PHE SER LYS SER GLU LEU ALA SER ALA
SEQRES 7 C 195 VAL LEU GLU ALA VAL GLU ASN ASN THR LEU SER ILE GLU
SEQRES 8 C 195 PRO VAL GLY LEU GLN PRO ILE ARG PHE VAL LYS ALA SER
SEQRES 9 C 195 ALA VAL GLU CYS GLY GLY PRO LYS LYS CYS ALA LEU THR
SEQRES 10 C 195 GLY GLN SER LYS SER CYS LYS HIS ARG ILE LYS LEU GLY
SEQRES 11 C 195 ASP SER SER ASN TYR TYR TYR ILE SER PRO PHE CYS ARG
SEQRES 12 C 195 TYR ARG ILE THR SER VAL CYS ASN PHE PHE THR TYR ILE
SEQRES 13 C 195 ARG TYR ILE GLN GLN GLY LEU VAL LYS GLN GLN ASP VAL
SEQRES 14 C 195 ASP GLN MET PHE TRP GLU VAL MET GLN LEU ARG LYS GLU
SEQRES 15 C 195 MET SER LEU ALA LYS LEU GLY TYR PHE LYS GLU GLU LEU
SEQRES 1 D 195 GLY ALA ALA SER ASN LYS SER THR SER SER ALA MET SER
SEQRES 2 D 195 GLY SER HIS GLN ASP LEU SER VAL ILE GLN PRO ILE VAL
SEQRES 3 D 195 LYS ASP CYS LYS GLU ALA ASP LEU SER LEU TYR ASN GLU
SEQRES 4 D 195 PHE ARG LEU TRP LYS ASP GLU PRO THR MET ASP ARG THR
SEQRES 5 D 195 CYS PRO PHE LEU ASP LYS ILE TYR GLN GLU ASP ILE PHE
SEQRES 6 D 195 PRO CYS LEU THR PHE SER LYS SER GLU LEU ALA SER ALA
SEQRES 7 D 195 VAL LEU GLU ALA VAL GLU ASN ASN THR LEU SER ILE GLU
SEQRES 8 D 195 PRO VAL GLY LEU GLN PRO ILE ARG PHE VAL LYS ALA SER
SEQRES 9 D 195 ALA VAL GLU CYS GLY GLY PRO LYS LYS CYS ALA LEU THR
SEQRES 10 D 195 GLY GLN SER LYS SER CYS LYS HIS ARG ILE LYS LEU GLY
SEQRES 11 D 195 ASP SER SER ASN TYR TYR TYR ILE SER PRO PHE CYS ARG
SEQRES 12 D 195 TYR ARG ILE THR SER VAL CYS ASN PHE PHE THR TYR ILE
SEQRES 13 D 195 ARG TYR ILE GLN GLN GLY LEU VAL LYS GLN GLN ASP VAL
SEQRES 14 D 195 ASP GLN MET PHE TRP GLU VAL MET GLN LEU ARG LYS GLU
SEQRES 15 D 195 MET SER LEU ALA LYS LEU GLY TYR PHE LYS GLU GLU LEU
HET GNP A 201 32
HET MG A 202 1
HET SO4 A 203 5
HET GNP B 201 32
HET MG B 202 1
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
FORMUL 5 GNP 2(C10 H17 N6 O13 P3)
FORMUL 6 MG 2(MG 2+)
FORMUL 7 SO4 O4 S 2-
FORMUL 10 HOH *159(H2 O)
HELIX 1 1 GLY A 23 ARG A 33 1 11
HELIX 2 2 THR A 77 ARG A 82 1 6
HELIX 3 3 LYS A 95 ASN A 101 1 7
HELIX 4 4 ASN A 101 HIS A 112 1 12
HELIX 5 5 PRO A 135 ASN A 146 1 12
HELIX 6 6 ASN A 160 GLN A 178 1 19
HELIX 7 7 GLY B 23 ARG B 33 1 11
HELIX 8 8 LYS B 95 ASN B 101 1 7
HELIX 9 9 ASN B 101 HIS B 112 1 12
HELIX 10 10 PRO B 135 ASN B 146 1 12
HELIX 11 11 ASN B 160 ILE B 175 1 16
HELIX 12 12 ASP C 298 ASP C 310 1 13
HELIX 13 13 CYS C 318 ASP C 328 1 11
HELIX 14 14 ASP C 328 LEU C 333 1 6
HELIX 15 15 LYS C 337 ASN C 350 1 14
HELIX 16 16 SER C 404 GLN C 426 1 23
HELIX 17 17 ASP C 433 LEU C 453 1 21
HELIX 18 18 ASP D 298 ASP D 310 1 13
HELIX 19 19 CYS D 318 ASP D 328 1 11
HELIX 20 20 ASP D 328 LEU D 333 1 6
HELIX 21 21 LYS D 337 ASN D 350 1 14
HELIX 22 22 SER D 404 GLN D 426 1 23
HELIX 23 23 ASP D 433 LEU D 453 1 21
SHEET 1 AA 6 VAL A 46 VAL A 55 0
SHEET 2 AA 6 LYS A 58 THR A 67 -1 O LYS A 58 N VAL A 55
SHEET 3 AA 6 TYR A 10 GLY A 18 1 O TYR A 10 N LYS A 61
SHEET 4 AA 6 GLY A 86 ASP A 92 1 O GLY A 86 N VAL A 15
SHEET 5 AA 6 VAL A 118 ASN A 124 1 O VAL A 118 N ALA A 87
SHEET 6 AA 6 SER A 149 GLU A 152 1 O SER A 149 N LEU A 121
SHEET 1 BA 6 VAL B 46 VAL B 55 0
SHEET 2 BA 6 LYS B 58 THR B 67 -1 O LYS B 58 N VAL B 55
SHEET 3 BA 6 TYR B 10 ILE B 17 1 O TYR B 10 N LYS B 61
SHEET 4 BA 6 GLY B 86 ASP B 92 1 O GLY B 86 N VAL B 15
SHEET 5 BA 6 VAL B 118 ASN B 124 1 O VAL B 118 N ALA B 87
SHEET 6 BA 6 SER B 149 GLU B 152 1 O SER B 149 N LEU B 121
SHEET 1 CA 3 SER C 354 PRO C 357 0
SHEET 2 CA 3 HIS C 390 LYS C 393 -1 O ARG C 391 N GLU C 356
SHEET 3 CA 3 TYR C 400 ILE C 403 -1 O TYR C 401 N ILE C 392
SHEET 1 DA 3 SER D 354 PRO D 357 0
SHEET 2 DA 3 HIS D 390 LYS D 393 -1 O ARG D 391 N GLU D 356
SHEET 3 DA 3 TYR D 400 ILE D 403 -1 O TYR D 401 N ILE D 392
LINK OG SER A 25 MG MG A 202 1555 1555 2.14
LINK OG1 THR A 43 MG MG A 202 1555 1555 2.04
LINK O3G GNP A 201 MG MG A 202 1555 1555 1.95
LINK O2B GNP A 201 MG MG A 202 1555 1555 1.95
LINK MG MG A 202 O HOH A2006 1555 1555 2.28
LINK MG MG A 202 O HOH A2007 1555 1555 2.24
LINK OG SER B 25 MG MG B 202 1555 1555 1.94
LINK OG1 THR B 43 MG MG B 202 1555 1555 2.58
LINK O2B GNP B 201 MG MG B 202 1555 1555 2.50
LINK O3G GNP B 201 MG MG B 202 1555 1555 2.52
LINK MG MG B 202 O HOH B2006 1555 1555 2.27
LINK MG MG B 202 O HOH B2007 1555 1555 2.04
CISPEP 1 VAL A 122 GLY A 123 0 9.59
CISPEP 2 ASP C 396 SER C 397 0 14.75
SITE 1 AC1 27 SER A 20 GLY A 21 VAL A 22 GLY A 23
SITE 2 AC1 27 LYS A 24 SER A 25 ASN A 26 PHE A 36
SITE 3 AC1 27 ASN A 37 LEU A 38 SER A 40 SER A 42
SITE 4 AC1 27 THR A 43 ALA A 68 GLY A 69 ASN A 124
SITE 5 AC1 27 LYS A 125 ASP A 127 LEU A 128 SER A 154
SITE 6 AC1 27 ALA A 155 LEU A 156 MG A 202 HOH A2006
SITE 7 AC1 27 HOH A2007 HOH A2027 TYR C 423
SITE 1 AC2 6 SER A 25 THR A 43 ASP A 66 GNP A 201
SITE 2 AC2 6 HOH A2006 HOH A2007
SITE 1 AC3 4 ASP A 92 ALA A 94 LYS A 95 LYS A 125
SITE 1 AC4 27 SER B 20 GLY B 21 VAL B 22 GLY B 23
SITE 2 AC4 27 LYS B 24 SER B 25 ASN B 26 PHE B 36
SITE 3 AC4 27 ASN B 37 LEU B 38 SER B 40 SER B 42
SITE 4 AC4 27 THR B 43 THR B 67 ALA B 68 GLY B 69
SITE 5 AC4 27 ASN B 124 LYS B 125 ASP B 127 LEU B 128
SITE 6 AC4 27 SER B 154 ALA B 155 LEU B 156 MG B 202
SITE 7 AC4 27 HOH B2006 HOH B2007 TYR D 423
SITE 1 AC5 5 SER B 25 THR B 43 GNP B 201 HOH B2006
SITE 2 AC5 5 HOH B2007
CRYST1 51.683 108.202 75.736 90.00 102.83 90.00 P 1 21 1 4
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 0.019349 0.000000 0.004407 0.00000
SCALE2 0.000000 0.009242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013542 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
