HEADER SIGNALING PROTEIN 10-JAN-06 2FN4
TITLE THE CRYSTAL STRUCTURE OF HUMAN RAS-RELATED PROTEIN, RRAS, IN THE GDP-
TITLE 2 BOUND STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED PROTEIN R-RAS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 23-201;
COMPND 5 SYNONYM: P23;
COMPND 6 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: RRAS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3)R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS RRAS, GDP/GTP BINDING, GTP HYDROLYSIS, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.P.TURNBULL,J.M.ELKINS,C.GILEADI,N.BURGESS,E.SALAH,E.PAPAGRIGORIOU,
AUTHOR 2 J.DEBRECZENI,F.VON DELFT,J.WEIGELT,A.EDWARDS,C.ARROWSMITH,
AUTHOR 3 M.SUNDSTROM,D.DOYLE,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 30-AUG-23 2FN4 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2FN4 1 VERSN
REVDAT 3 28-APR-10 2FN4 1 AUTHOR JRNL
REVDAT 2 24-FEB-09 2FN4 1 VERSN
REVDAT 1 31-JAN-06 2FN4 0
JRNL AUTH A.P.TURNBULL,J.M.ELKINS,C.GILEADI,N.BURGESS,E.SALAH,
JRNL AUTH 2 E.PAPAGRIGORIOU,J.DEBRECZENI,F.VON DELFT,J.WEIGELT,
JRNL AUTH 3 A.EDWARDS,C.ARROWSMITH,M.SUNDSTROM,D.DOYLE
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN RAS-RELATED PROTEIN, RRAS, IN
JRNL TITL 2 THE GDP-BOUND STATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 19180
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1039
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1446
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1344
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.33000
REMARK 3 B33 (A**2) : -0.49000
REMARK 3 B12 (A**2) : 0.16000
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): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.224
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1411 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 949 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1917 ; 1.390 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2295 ; 0.936 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 174 ; 6.168 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 70 ;29.789 ;23.571
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 223 ;13.135 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.926 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 210 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1588 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 308 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 281 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1033 ; 0.205 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 700 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 742 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 84 ; 0.163 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.160 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.184 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 23 ; 0.224 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.183 ; 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): 927 ; 0.776 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 355 ; 0.198 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1384 ; 1.077 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 599 ; 1.741 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 532 ; 2.585 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 24 A 96
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7335 29.4233 18.2970
REMARK 3 T TENSOR
REMARK 3 T11: -0.0680 T22: 0.2258
REMARK 3 T33: -0.1171 T12: 0.0281
REMARK 3 T13: 0.0285 T23: 0.0963
REMARK 3 L TENSOR
REMARK 3 L11: 3.6860 L22: 3.2040
REMARK 3 L33: 3.5745 L12: 0.2655
REMARK 3 L13: -0.1999 L23: 0.0325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0678 S12: -1.0051 S13: -0.1337
REMARK 3 S21: 0.5134 S22: -0.1210 S23: -0.1763
REMARK 3 S31: 0.2643 S32: 0.4944 S33: 0.0533
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 97 A 196
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8945 38.1252 9.0429
REMARK 3 T TENSOR
REMARK 3 T11: -0.2168 T22: -0.0565
REMARK 3 T33: -0.1530 T12: -0.0015
REMARK 3 T13: 0.0508 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 3.7043 L22: 3.0817
REMARK 3 L33: 3.2264 L12: 1.0275
REMARK 3 L13: -0.5214 L23: -0.1257
REMARK 3 S TENSOR
REMARK 3 S11: 0.1143 S12: -0.5526 S13: 0.3133
REMARK 3 S21: 0.1285 S22: -0.2222 S23: 0.0964
REMARK 3 S31: -0.2167 S32: 0.3086 S33: 0.1079
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 2FN4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036073.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00008
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20362
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
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 (%) : 95.7
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 2ERY.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M NA/KPO4, 0.1M HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.83300
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 103.66600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 103.66600
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 51.83300
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SER A 21
REMARK 465 MET A 22
REMARK 465 ASP A 23
REMARK 465 GLU A 197
REMARK 465 LEU A 198
REMARK 465 PRO A 199
REMARK 465 PRO A 200
REMARK 465 SER A 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 LYS A 31 CD CE NZ
REMARK 470 GLN A 96 CD OE1 NE2
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 LYS A 121 CD CE NZ
REMARK 470 LYS A 192 CD CE NZ
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 OD1 ASP A 73 O HOH A 265 2.11
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 PRO A 25 160.03 -47.40
REMARK 500 PRO A 26 -110.88 -87.10
REMARK 500 GLU A 28 39.92 -95.13
REMARK 500 ASP A 57 49.47 -143.24
REMARK 500 ASP A 59 102.56 -17.53
REMARK 500 GLU A 89 -42.13 -136.84
REMARK 500 LYS A 143 37.67 72.01
REMARK 500 LEU A 146 44.62 -109.91
REMARK 500
REMARK 500 REMARK: NULL
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 2 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP A 1 O2B
REMARK 620 2 SER A 43 OG 88.4
REMARK 620 3 HOH A 230 O 87.8 176.1
REMARK 620 4 HOH A 236 O 86.5 84.1 94.7
REMARK 620 5 HOH A 240 O 175.5 93.3 90.5 89.6
REMARK 620 6 HOH A 249 O 99.9 86.9 94.7 168.8 84.3
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 MG A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 1
DBREF 2FN4 A 23 201 UNP P10301 RRAS_HUMAN 23 201
SEQADV 2FN4 SER A 21 UNP P10301 CLONING ARTIFACT
SEQADV 2FN4 MET A 22 UNP P10301 CLONING ARTIFACT
SEQRES 1 A 181 SER MET ASP PRO PRO PRO SER GLU THR HIS LYS LEU VAL
SEQRES 2 A 181 VAL VAL GLY GLY GLY GLY VAL GLY LYS SER ALA LEU THR
SEQRES 3 A 181 ILE GLN PHE ILE GLN SER TYR PHE VAL SER ASP TYR ASP
SEQRES 4 A 181 PRO THR ILE GLU ASP SER TYR THR LYS ILE CYS SER VAL
SEQRES 5 A 181 ASP GLY ILE PRO ALA ARG LEU ASP ILE LEU ASP THR ALA
SEQRES 6 A 181 GLY GLN GLU GLU PHE GLY ALA MET ARG GLU GLN TYR MET
SEQRES 7 A 181 ARG ALA GLY HIS GLY PHE LEU LEU VAL PHE ALA ILE ASN
SEQRES 8 A 181 ASP ARG GLN SER PHE ASN GLU VAL GLY LYS LEU PHE THR
SEQRES 9 A 181 GLN ILE LEU ARG VAL LYS ASP ARG ASP ASP PHE PRO VAL
SEQRES 10 A 181 VAL LEU VAL GLY ASN LYS ALA ASP LEU GLU SER GLN ARG
SEQRES 11 A 181 GLN VAL PRO ARG SER GLU ALA SER ALA PHE GLY ALA SER
SEQRES 12 A 181 HIS HIS VAL ALA TYR PHE GLU ALA SER ALA LYS LEU ARG
SEQRES 13 A 181 LEU ASN VAL ASP GLU ALA PHE GLU GLN LEU VAL ARG ALA
SEQRES 14 A 181 VAL ARG LYS TYR GLN GLU GLN GLU LEU PRO PRO SER
HET MG A 2 1
HET GDP A 1 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 GDP C10 H15 N5 O11 P2
FORMUL 4 HOH *94(H2 O)
HELIX 1 1 GLY A 41 SER A 52 1 12
HELIX 2 2 MET A 93 GLY A 101 1 9
HELIX 3 3 ASP A 112 ASP A 131 1 20
HELIX 4 4 LYS A 143 ARG A 150 5 8
HELIX 5 5 PRO A 153 HIS A 164 1 12
HELIX 6 6 ASN A 178 GLN A 194 1 17
SHEET 1 A 6 ASP A 64 VAL A 72 0
SHEET 2 A 6 ILE A 75 ASP A 83 -1 O LEU A 79 N LYS A 68
SHEET 3 A 6 THR A 29 GLY A 36 1 N HIS A 30 O ARG A 78
SHEET 4 A 6 GLY A 103 ALA A 109 1 O VAL A 107 N VAL A 35
SHEET 5 A 6 VAL A 137 ASN A 142 1 O ASN A 142 N PHE A 108
SHEET 6 A 6 ALA A 167 GLU A 170 1 O PHE A 169 N GLY A 141
LINK O2B GDP A 1 MG MG A 2 1555 1555 2.08
LINK MG MG A 2 OG SER A 43 1555 1555 2.11
LINK MG MG A 2 O HOH A 230 1555 1555 2.08
LINK MG MG A 2 O HOH A 236 1555 1555 2.38
LINK MG MG A 2 O HOH A 240 1555 1555 2.17
LINK MG MG A 2 O HOH A 249 1555 1555 1.83
SITE 1 AC1 6 GDP A 1 SER A 43 HOH A 230 HOH A 236
SITE 2 AC1 6 HOH A 240 HOH A 249
SITE 1 AC2 24 MG A 2 GLY A 39 VAL A 40 GLY A 41
SITE 2 AC2 24 LYS A 42 SER A 43 ALA A 44 SER A 56
SITE 3 AC2 24 ASN A 142 LYS A 143 ASP A 145 LEU A 146
SITE 4 AC2 24 SER A 172 ALA A 173 LYS A 174 HOH A 230
SITE 5 AC2 24 HOH A 236 HOH A 249 HOH A 251 HOH A 267
SITE 6 AC2 24 HOH A 268 HOH A 277 HOH A 283 HOH A 293
CRYST1 43.152 43.152 155.499 90.00 90.00 120.00 P 31 2 1 6
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 0.023174 0.013379 0.000000 0.00000
SCALE2 0.000000 0.026759 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006431 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
