HEADER SIGNALING PROTEIN 16-JUL-15 5CM8
TITLE STRUCTURAL BASIS FOR THE SELECTIVITY OF GUANINE NUCLEOTIDE EXCHANGE
TITLE 2 FACTORS FOR THE SMALL G-PROTEIN RAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAL GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR-LIKE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 50-514;
COMPND 5 SYNONYM: RALGDS-LIKE 2,RALGDS-LIKE FACTOR,RAS-ASSOCIATED PROTEIN
COMPND 6 RAB2L;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RAS-RELATED PROTEIN RAL-A;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: RAL;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RGL2, RAB2L, RLF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: CK600;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P3;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 13 ORGANISM_COMMON: FRUIT FLY;
SOURCE 14 ORGANISM_TAXID: 7227;
SOURCE 15 GENE: RALA, CG2849;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: CK600;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX4T3
KEYWDS COMPLEX G-PROTEIN EXCHANGE FACTOR, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.POPOVIC,A.SCHOUTEN,H.REHMANN
REVDAT 3 10-JAN-24 5CM8 1 REMARK
REVDAT 2 03-FEB-16 5CM8 1 JRNL
REVDAT 1 13-JAN-16 5CM8 0
JRNL AUTH M.POPOVIC,A.SCHOUTEN,M.RENSEN-DE LEEUW,H.REHMANN
JRNL TITL THE STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF
JRNL TITL 2 IN COMPLEX WITH THE SMALL G-PROTEIN RAL IDENTIFIES
JRNL TITL 3 CONFORMATIONAL INTERMEDIATES OF THE EXCHANGE REACTION AND
JRNL TITL 4 THE BASIS FOR THE SELECTIVITY.
JRNL REF J.STRUCT.BIOL. V. 193 106 2016
JRNL REFN ESSN 1095-8657
JRNL PMID 26687416
JRNL DOI 10.1016/J.JSB.2015.12.006
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 22003
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 + TEST SET) : 0.262
REMARK 3 R VALUE (WORKING SET) : 0.259
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1159
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1654
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.3700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4589
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 45
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.13000
REMARK 3 B22 (A**2) : 4.09000
REMARK 3 B33 (A**2) : -2.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.792
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.391
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.329
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.198
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.864
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4677 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6338 ; 0.927 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 582 ; 4.506 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 221 ;34.415 ;22.896
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 776 ;17.457 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;14.241 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 712 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3578 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2927 ; 0.339 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4694 ; 0.630 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1750 ; 0.637 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1644 ; 1.165 ; 4.500
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
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 5CM8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211857.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.45
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23162
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.210
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4JGW AS POLY ALA MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 200 MM AMMONIUM ACETATE,
REMARK 280 100 MM BIS-TRIS PROPANE, PH 7.45, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 55.55500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.24500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 55.55500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.24500
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 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 GLY A 42
REMARK 465 PRO A 43
REMARK 465 LEU A 44
REMARK 465 GLY A 45
REMARK 465 SER A 46
REMARK 465 PRO A 47
REMARK 465 ASN A 48
REMARK 465 SER A 49
REMARK 465 GLU A 50
REMARK 465 GLU A 51
REMARK 465 GLU A 52
REMARK 465 ALA A 53
REMARK 465 ALA A 196
REMARK 465 ARG A 197
REMARK 465 GLU A 198
REMARK 465 GLY A 199
REMARK 465 VAL A 200
REMARK 465 VAL A 201
REMARK 465 GLY A 202
REMARK 465 VAL A 215
REMARK 465 ASP A 216
REMARK 465 PRO A 217
REMARK 465 ARG A 218
REMARK 465 ALA A 219
REMARK 465 PRO A 220
REMARK 465 ASP A 221
REMARK 465 LEU A 222
REMARK 465 PRO A 223
REMARK 465 LYS A 224
REMARK 465 PRO A 225
REMARK 465 LEU A 226
REMARK 465 ALA A 227
REMARK 465 LEU A 228
REMARK 465 PRO A 229
REMARK 465 GLY A 230
REMARK 465 ASP A 231
REMARK 465 SER A 232
REMARK 465 GLN A 403
REMARK 465 GLU A 404
REMARK 465 VAL A 405
REMARK 465 LYS A 406
REMARK 465 PRO A 407
REMARK 465 GLN A 408
REMARK 465 PRO A 409
REMARK 465 PRO A 410
REMARK 465 VAL A 411
REMARK 465 GLU A 412
REMARK 465 PRO A 413
REMARK 465 HIS A 414
REMARK 465 SER A 415
REMARK 465 LYS A 416
REMARK 465 LYS A 417
REMARK 465 ALA A 418
REMARK 465 PRO A 419
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 LYS B 4
REMARK 465 PRO B 5
REMARK 465 THR B 6
REMARK 465 ALA B 7
REMARK 465 CYS B 126
REMARK 465 ASP B 127
REMARK 465 LEU B 128
REMARK 465 SER B 180
REMARK 465 LYS B 181
REMARK 465 ALA B 182
REMARK 465 THR B 183
REMARK 465 SER B 184
REMARK 465 GLY B 185
REMARK 465 ARG B 186
REMARK 465 ALA B 187
REMARK 465 LYS B 188
REMARK 465 ASP B 189
REMARK 465 ARG B 190
REMARK 465 CYS B 191
REMARK 465 LYS B 192
REMARK 465 LYS B 193
REMARK 465 ARG B 194
REMARK 465 ARG B 195
REMARK 465 LEU B 196
REMARK 465 LYS B 197
REMARK 465 CYS B 198
REMARK 465 THR B 199
REMARK 465 LEU B 200
REMARK 465 LEU B 201
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 GLU B 35 CG CD OE1 OE2
REMARK 470 ASP B 95 CG OD1 OD2
REMARK 470 ASN B 129 CG OD1 ND2
REMARK 470 LYS B 131 CG CD CE NZ
REMARK 470 ARG B 132 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 133 CG CD CE NZ
REMARK 470 VAL B 134 CG1 CG2
REMARK 470 PRO B 135 CG CD
REMARK 470 LEU B 136 CG CD1 CD2
REMARK 470 SER B 137 OG
REMARK 470 GLU B 138 CG CD OE1 OE2
REMARK 470 GLN B 140 CG CD OE1 NE2
REMARK 470 LEU B 141 CG CD1 CD2
REMARK 470 GLU B 152 CG CD OE1 OE2
REMARK 470 LYS B 163 CG CD CE NZ
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 ASP A 63 -71.72 -11.62
REMARK 500 ALA A 112 -77.79 -94.08
REMARK 500 ASP A 238 1.58 -69.92
REMARK 500 ASP B 34 -92.85 -99.90
REMARK 500 PHE B 36 54.08 -118.12
REMARK 500 ASN B 113 31.25 -94.10
REMARK 500 PRO B 118 117.75 -35.40
REMARK 500 ASN B 124 -143.43 -101.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CM9 RELATED DB: PDB
DBREF 5CM8 A 50 514 UNP Q61193 RGL2_MOUSE 50 514
DBREF 5CM8 B 1 201 UNP P48555 RALA_DROME 1 201
SEQADV 5CM8 GLY A 42 UNP Q61193 EXPRESSION TAG
SEQADV 5CM8 PRO A 43 UNP Q61193 EXPRESSION TAG
SEQADV 5CM8 LEU A 44 UNP Q61193 EXPRESSION TAG
SEQADV 5CM8 GLY A 45 UNP Q61193 EXPRESSION TAG
SEQADV 5CM8 SER A 46 UNP Q61193 EXPRESSION TAG
SEQADV 5CM8 PRO A 47 UNP Q61193 EXPRESSION TAG
SEQADV 5CM8 ASN A 48 UNP Q61193 EXPRESSION TAG
SEQADV 5CM8 SER A 49 UNP Q61193 EXPRESSION TAG
SEQADV 5CM8 TYR A 147 UNP Q61193 HIS 147 CONFLICT
SEQADV 5CM8 THR A 402 UNP Q61193 MET 402 CONFLICT
SEQADV 5CM8 GLY B -1 UNP P48555 EXPRESSION TAG
SEQADV 5CM8 SER B 0 UNP P48555 EXPRESSION TAG
SEQRES 1 A 473 GLY PRO LEU GLY SER PRO ASN SER GLU GLU GLU ALA SER
SEQRES 2 A 473 VAL SER VAL TRP ASP GLU GLU GLU ASP GLY ALA THR PHE
SEQRES 3 A 473 THR VAL THR SER ARG GLN TYR ARG PRO LEU ASP PRO LEU
SEQRES 4 A 473 ALA PRO LEU PRO PRO PRO ARG SER SER ARG ARG LEU ARG
SEQRES 5 A 473 ALA GLY THR LEU GLU ALA LEU VAL ARG HIS LEU LEU ASP
SEQRES 6 A 473 ALA ARG THR ALA GLY ALA ASP MET MET PHE THR PRO ALA
SEQRES 7 A 473 LEU LEU ALA THR HIS ARG ALA PHE THR SER THR PRO ALA
SEQRES 8 A 473 LEU PHE GLY LEU VAL ALA ASP ARG LEU GLU ALA LEU GLU
SEQRES 9 A 473 SER TYR PRO PRO GLY GLU LEU GLU ARG THR THR GLY VAL
SEQRES 10 A 473 ALA ILE SER VAL LEU SER THR TRP LEU ALA SER HIS PRO
SEQRES 11 A 473 GLU ASP PHE GLY SER GLU VAL LYS GLY GLN LEU ASP ARG
SEQRES 12 A 473 LEU GLU SER PHE LEU LEU ARG THR GLY TYR ALA ALA ARG
SEQRES 13 A 473 GLU GLY VAL VAL GLY GLY SER ALA ASP LEU ILE ARG ASN
SEQRES 14 A 473 LEU ARG ALA ARG VAL ASP PRO ARG ALA PRO ASP LEU PRO
SEQRES 15 A 473 LYS PRO LEU ALA LEU PRO GLY ASP SER PRO ALA ASP PRO
SEQRES 16 A 473 THR ASP VAL LEU VAL PHE LEU ALA ASP HIS LEU ALA GLU
SEQRES 17 A 473 GLN LEU THR LEU LEU ASP ALA GLU LEU PHE LEU ASN LEU
SEQRES 18 A 473 ILE PRO SER GLN CYS LEU GLY GLY LEU TRP GLY HIS ARG
SEQRES 19 A 473 ASP ARG PRO GLY HIS SER HIS LEU CYS PRO SER VAL ARG
SEQRES 20 A 473 ALA THR VAL THR GLN PHE ASN LYS VAL ALA GLY ALA VAL
SEQRES 21 A 473 VAL SER SER VAL LEU GLY ALA THR SER ILE GLY GLU GLY
SEQRES 22 A 473 PRO ARG GLU VAL THR VAL ARG PRO LEU ARG PRO PRO GLN
SEQRES 23 A 473 ARG ALA ARG LEU LEU GLU LYS TRP ILE ARG VAL ALA GLU
SEQRES 24 A 473 GLU CYS ARG LEU LEU ARG ASN PHE SER SER VAL TYR ALA
SEQRES 25 A 473 VAL VAL SER ALA LEU GLN SER SER PRO ILE HIS ARG LEU
SEQRES 26 A 473 ARG ALA ALA TRP GLY GLU THR THR ARG ASP SER LEU ARG
SEQRES 27 A 473 VAL PHE SER SER LEU CYS GLN ILE PHE SER GLU GLU ASP
SEQRES 28 A 473 ASN TYR SER GLN SER ARG GLU LEU LEU THR GLN GLU VAL
SEQRES 29 A 473 LYS PRO GLN PRO PRO VAL GLU PRO HIS SER LYS LYS ALA
SEQRES 30 A 473 PRO ARG SER GLY PHE ARG GLY GLY GLY VAL VAL PRO TYR
SEQRES 31 A 473 LEU GLY THR PHE LEU LYS ASP LEU VAL MET LEU ASP ALA
SEQRES 32 A 473 ALA SER LYS ASP GLU LEU GLU ASN GLY TYR ILE ASN PHE
SEQRES 33 A 473 ASP LYS ARG ARG LYS GLU PHE ALA ILE LEU SER GLU LEU
SEQRES 34 A 473 LEU ARG LEU GLN LYS GLU CYS ARG GLY TYR ASP LEU ARG
SEQRES 35 A 473 PRO ASN SER ASP ILE GLN GLN TRP LEU GLN GLY LEU GLN
SEQRES 36 A 473 PRO LEU THR GLU ALA GLN SER HIS ARG VAL SER CYS GLU
SEQRES 37 A 473 VAL GLU PRO PRO GLY
SEQRES 1 B 203 GLY SER MET SER LYS LYS PRO THR ALA GLY PRO ALA LEU
SEQRES 2 B 203 HIS LYS VAL ILE MET VAL GLY SER GLY GLY VAL GLY LYS
SEQRES 3 B 203 SER ALA LEU THR LEU GLN PHE MET TYR ASP GLU PHE VAL
SEQRES 4 B 203 GLU ASP TYR GLU PRO THR LYS ALA ASP SER TYR ARG LYS
SEQRES 5 B 203 LYS VAL VAL LEU ASP GLY GLU GLU VAL GLN ILE ASP ILE
SEQRES 6 B 203 LEU ASP THR ALA GLY GLN GLU ASP TYR ALA ALA ILE ARG
SEQRES 7 B 203 ASP ASN TYR PHE ARG SER GLY GLU GLY PHE LEU CYS VAL
SEQRES 8 B 203 PHE SER ILE THR ASP ASP GLU SER PHE GLN ALA THR GLN
SEQRES 9 B 203 GLU PHE ARG GLU GLN ILE LEU ARG VAL LYS ASN ASP GLU
SEQRES 10 B 203 SER ILE PRO PHE LEU LEU VAL GLY ASN LYS CYS ASP LEU
SEQRES 11 B 203 ASN ASP LYS ARG LYS VAL PRO LEU SER GLU CYS GLN LEU
SEQRES 12 B 203 ARG ALA GLN GLN TRP ALA VAL PRO TYR VAL GLU THR SER
SEQRES 13 B 203 ALA LYS THR ARG GLU ASN VAL ASP LYS VAL PHE PHE ASP
SEQRES 14 B 203 LEU MET ARG GLU ILE ARG SER ARG LYS THR GLU ASP SER
SEQRES 15 B 203 LYS ALA THR SER GLY ARG ALA LYS ASP ARG CYS LYS LYS
SEQRES 16 B 203 ARG ARG LEU LYS CYS THR LEU LEU
FORMUL 3 HOH *45(H2 O)
HELIX 1 AA1 THR A 96 LEU A 105 1 10
HELIX 2 AA2 MET A 115 HIS A 124 1 10
HELIX 3 AA3 ARG A 125 PHE A 127 5 3
HELIX 4 AA4 SER A 129 ALA A 143 1 15
HELIX 5 AA5 PRO A 148 HIS A 170 1 23
HELIX 6 AA6 PRO A 171 PHE A 174 5 4
HELIX 7 AA7 GLY A 175 GLU A 177 5 3
HELIX 8 AA8 VAL A 178 THR A 192 1 15
HELIX 9 AA9 SER A 204 ALA A 213 1 10
HELIX 10 AB1 ASP A 235 PHE A 242 5 8
HELIX 11 AB2 LEU A 243 ASN A 261 1 19
HELIX 12 AB3 ILE A 263 CYS A 267 5 5
HELIX 13 AB4 LEU A 268 GLY A 273 1 6
HELIX 14 AB5 CYS A 284 LEU A 306 1 23
HELIX 15 AB6 ARG A 324 ARG A 346 1 23
HELIX 16 AB7 ASN A 347 SER A 360 1 14
HELIX 17 AB8 SER A 360 ARG A 365 1 6
HELIX 18 AB9 LEU A 366 GLU A 372 1 7
HELIX 19 AC1 THR A 374 PHE A 388 1 15
HELIX 20 AC2 GLU A 390 THR A 402 1 13
HELIX 21 AC3 LEU A 432 SER A 446 1 15
HELIX 22 AC4 PHE A 457 ARG A 478 1 22
HELIX 23 AC5 ASN A 485 GLY A 494 1 10
HELIX 24 AC6 THR A 499 GLU A 511 1 13
HELIX 25 AC7 GLY B 23 TYR B 33 1 11
HELIX 26 AC8 ALA B 74 ARG B 81 1 8
HELIX 27 AC9 ASP B 95 ALA B 100 1 6
HELIX 28 AD1 ALA B 100 ARG B 110 1 11
HELIX 29 AD2 PRO B 135 GLN B 144 1 10
HELIX 30 AD3 GLN B 145 ALA B 147 5 3
HELIX 31 AD4 ASN B 160 GLU B 178 1 19
SHEET 1 AA1 4 VAL A 55 GLU A 62 0
SHEET 2 AA1 4 ALA A 65 ARG A 72 -1 O SER A 71 N SER A 56
SHEET 3 AA1 4 ARG A 87 GLY A 95 -1 O ARG A 93 N THR A 66
SHEET 4 AA1 4 ILE A 455 ASN A 456 -1 O ILE A 455 N GLY A 95
SHEET 1 AA2 2 ALA A 308 SER A 310 0
SHEET 2 AA2 2 VAL A 318 VAL A 320 -1 O THR A 319 N THR A 309
SHEET 1 AA3 6 ARG B 49 LEU B 54 0
SHEET 2 AA3 6 GLU B 57 ASP B 65 -1 O VAL B 59 N VAL B 52
SHEET 3 AA3 6 LEU B 11 VAL B 17 1 N HIS B 12 O ASP B 62
SHEET 4 AA3 6 GLY B 85 PHE B 90 1 O GLY B 85 N LYS B 13
SHEET 5 AA3 6 PHE B 119 GLY B 123 1 O LEU B 120 N CYS B 88
SHEET 6 AA3 6 TYR B 150 GLU B 152 1 O VAL B 151 N LEU B 121
CISPEP 1 ARG B 81 SER B 82 0 2.80
CRYST1 111.110 98.490 71.320 90.00 91.61 90.00 C 1 2 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 0.009000 0.000000 0.000252 0.00000
SCALE2 0.000000 0.010153 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014027 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
