HEADER HYDROLASE 19-JUL-10 2L0X
TITLE SOLUTION STRUCTURE OF THE 21 KDA GTPASE RHEB BOUND TO GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING PROTEIN RHEB;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RAS HOMOLOG ENRICHED IN BRAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: RHEB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-30
KEYWDS GTPASE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.STOLL,R.HEUMANN,C.BERGHAUS,G.KOCK
REVDAT 3 10-NOV-10 2L0X 1 JRNL
REVDAT 2 25-AUG-10 2L0X 1 JRNL
REVDAT 1 04-AUG-10 2L0X 0
JRNL AUTH S.KARASSEK,C.BERGHAUS,M.SCHWARTEN,C.G.GOEMANS,N.OHSE,G.KOCK,
JRNL AUTH 2 K.JOCKERS,S.NEUMANN,S.GOTTFRIED,C.HERRMANN,R.HEUMANN,R.STOLL
JRNL TITL RAS HOMOLOG ENRICHED IN BRAIN (RHEB) ENHANCES APOPTOTIC
JRNL TITL 2 SIGNALING.
JRNL REF J.BIOL.CHEM. V. 285 33979 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20685651
JRNL DOI 10.1074/JBC.M109.095968
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2L0X COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB101817.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9-1.2 MM [U-100% 13C; U-100%
REMARK 210 15N] PROTEIN, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-15N NOESY; 3D 1H-13C
REMARK 210 NOESY; 3D HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR_NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HG SER A 86 H THR A 88 1.32
REMARK 500 H SER A 86 HG SER A 92 1.33
REMARK 500 HZ2 LYS A 8 HE22 GLN A 57 1.36
REMARK 500 HG SER A 130 H GLU A 133 1.43
REMARK 500 H ASP A 65 HG SER A 68 1.44
REMARK 500 H SER A 149 HG1 THR A 155 1.44
REMARK 500 H GLY A 118 O LEU A 146 1.56
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 1 TYR A 14 -177.83 -49.31
REMARK 500 1 SER A 16 19.63 53.17
REMARK 500 1 SER A 34 96.28 33.21
REMARK 500 1 TYR A 35 41.87 -150.68
REMARK 500 1 PRO A 37 -139.62 -57.33
REMARK 500 1 ALA A 62 34.37 -144.79
REMARK 500 1 GLN A 64 -79.52 -123.26
REMARK 500 1 GLU A 66 -16.20 -45.20
REMARK 500 1 TYR A 67 -4.81 -175.56
REMARK 500 1 SER A 68 119.86 52.49
REMARK 500 1 GLN A 72 50.89 -174.59
REMARK 500 1 THR A 73 -6.67 77.34
REMARK 500 1 ILE A 76 -170.73 -51.87
REMARK 500 1 ASN A 79 17.62 -150.75
REMARK 500 1 THR A 88 -15.94 -141.92
REMARK 500 1 LYS A 109 -155.15 -93.33
REMARK 500 1 ARG A 127 88.00 38.91
REMARK 500 1 LYS A 151 5.64 -65.38
REMARK 500 1 ALA A 173 -80.55 -68.96
REMARK 500 2 TYR A 14 -158.35 -55.34
REMARK 500 2 PHE A 31 122.09 -39.88
REMARK 500 2 TYR A 35 85.91 -158.04
REMARK 500 2 PRO A 37 84.59 -26.69
REMARK 500 2 THR A 38 35.05 -68.65
REMARK 500 2 LYS A 45 117.13 -163.29
REMARK 500 2 ALA A 62 12.88 -140.66
REMARK 500 2 GLU A 66 -41.61 -21.82
REMARK 500 2 TYR A 67 5.00 -178.86
REMARK 500 2 SER A 68 93.97 36.67
REMARK 500 2 ILE A 76 -169.16 -50.53
REMARK 500 2 ASP A 77 54.28 -117.29
REMARK 500 2 ASN A 79 17.33 -151.19
REMARK 500 2 VAL A 87 21.87 -73.69
REMARK 500 2 ILE A 90 -8.40 -59.37
REMARK 500 2 LYS A 109 94.51 83.85
REMARK 500 2 PRO A 113 101.81 -51.83
REMARK 500 2 HIS A 124 -25.78 -37.53
REMARK 500 2 ARG A 127 90.65 26.68
REMARK 500 2 TYR A 131 -39.56 -39.23
REMARK 500 2 ALA A 173 -81.63 -68.94
REMARK 500 3 TYR A 14 -159.03 -54.90
REMARK 500 3 PHE A 31 92.37 -68.05
REMARK 500 3 ASP A 33 26.75 -73.00
REMARK 500 3 SER A 34 64.05 -64.62
REMARK 500 3 PRO A 37 -137.68 -56.68
REMARK 500 3 ASN A 41 -179.00 -172.33
REMARK 500 3 ALA A 62 21.01 -143.17
REMARK 500 3 GLN A 64 -125.30 -145.31
REMARK 500 3 GLU A 66 56.00 -61.63
REMARK 500 3 TYR A 67 71.67 76.50
REMARK 500
REMARK 500 THIS ENTRY HAS 435 RAMACHANDRAN OUTLIERS.
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 1 MG A 185 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP A 186 O1B
REMARK 620 2 THR A 38 OG1 108.4
REMARK 620 3 SER A 20 OG 64.7 153.1
REMARK 620 N 1 2
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 185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 186
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 15048 RELATED DB: BMRB
DBREF 2L0X A 6 174 UNP Q62639 RHEB_RAT 6 174
SEQRES 1 A 169 SER ARG LYS ILE ALA ILE LEU GLY TYR ARG SER VAL GLY
SEQRES 2 A 169 LYS SER SER LEU THR ILE GLN PHE VAL GLU GLY GLN PHE
SEQRES 3 A 169 VAL ASP SER TYR ASP PRO THR ILE GLU ASN THR PHE THR
SEQRES 4 A 169 LYS LEU ILE THR VAL ASN GLY GLN GLU TYR HIS LEU GLN
SEQRES 5 A 169 LEU VAL ASP THR ALA GLY GLN ASP GLU TYR SER ILE PHE
SEQRES 6 A 169 PRO GLN THR TYR SER ILE ASP ILE ASN GLY TYR ILE LEU
SEQRES 7 A 169 VAL TYR SER VAL THR SER ILE LYS SER PHE GLU VAL ILE
SEQRES 8 A 169 LYS VAL ILE HIS GLY LYS LEU LEU ASP MET VAL GLY LYS
SEQRES 9 A 169 VAL GLN ILE PRO ILE MET LEU VAL GLY ASN LYS LYS ASP
SEQRES 10 A 169 LEU HIS MET GLU ARG VAL ILE SER TYR GLU GLU GLY LYS
SEQRES 11 A 169 ALA LEU ALA GLU SER TRP ASN ALA ALA PHE LEU GLU SER
SEQRES 12 A 169 SER ALA LYS GLU ASN GLN THR ALA VAL ASP VAL PHE ARG
SEQRES 13 A 169 ARG ILE ILE LEU GLU ALA GLU LYS ILE ASP GLY ALA ALA
HET MG A 185 1
HET GDP A 186 40
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 GDP C10 H15 N5 O11 P2
HELIX 1 1 GLY A 18 GLU A 28 1 11
HELIX 2 2 SER A 89 GLY A 108 1 20
HELIX 3 3 LYS A 120 HIS A 124 5 5
HELIX 4 4 SER A 130 ASN A 142 1 13
HELIX 5 5 GLU A 152 ALA A 174 1 23
SHEET 1 A 6 ASN A 41 VAL A 49 0
SHEET 2 A 6 GLN A 52 ASP A 60 -1 O LEU A 58 N PHE A 43
SHEET 3 A 6 ARG A 7 GLY A 13 1 N ILE A 11 O VAL A 59
SHEET 4 A 6 GLY A 80 SER A 86 1 O ILE A 82 N ALA A 10
SHEET 5 A 6 ILE A 114 ASN A 119 1 O MET A 115 N TYR A 81
SHEET 6 A 6 ALA A 144 GLU A 147 1 O LEU A 146 N GLY A 118
LINK MG MG A 185 O1B GDP A 186 1555 1555 2.41
LINK OG1 THR A 38 MG MG A 185 1555 1555 2.42
LINK OG SER A 20 MG MG A 185 1555 1555 2.43
SITE 1 AC1 3 SER A 20 THR A 38 GDP A 186
SITE 1 AC2 17 TYR A 14 SER A 16 VAL A 17 GLY A 18
SITE 2 AC2 17 LYS A 19 SER A 20 SER A 21 PRO A 37
SITE 3 AC2 17 THR A 38 ASN A 119 LYS A 120 ASP A 122
SITE 4 AC2 17 LEU A 123 SER A 149 ALA A 150 LYS A 151
SITE 5 AC2 17 MG A 185
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
