Header list of 1e0a.pdb file
Complete list - p 25 2 Bytes
HEADER SIGNALLING PROTEIN/KINASE 16-MAR-00 1E0A
TITLE CDC42 COMPLEXED WITH THE GTPASE BINDING DOMAIN OF P21 ACTIVATED KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION CONTROL PROTEIN 42 HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 1-184;
COMPND 5 SYNONYM: G25K GTP-BINDING PROTEIN;
COMPND 6 EC: 3.6.5.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: COMPLEXED WITH 5'-GUANOSYL-IMIDO-TRIPHOSPHATE;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PAK 1;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: 75-118;
COMPND 14 SYNONYM: ALPHA-PAK,PROTEIN KINASE MUK2,P21-ACTIVATED KINASE 1,PAK-1,
COMPND 15 P68-PAK;
COMPND 16 EC: 2.7.11.1;
COMPND 17 ENGINEERED: YES;
COMPND 18 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 GENE: CDC42;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 13 EXPRESSION_SYSTEM_GENE: CDC42;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 16 ORGANISM_COMMON: RAT;
SOURCE 17 ORGANISM_TAXID: 10116;
SOURCE 18 CELLULAR_LOCATION: CYTOPLASMIC;
SOURCE 19 GENE: PAK1;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 23 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 25 EXPRESSION_SYSTEM_PLASMID: PGEX2T;
SOURCE 26 EXPRESSION_SYSTEM_GENE: PAK
KEYWDS SIGNALLING PROTEIN, G PROTEIN SIGNALLING SER/THR KINASE, SIGNALLING
KEYWDS 2 PROTEIN-KINASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.MORREALE,M.VENKATESAN,H.R.MOTT,D.OWEN,D.NIETLISPACH,P.N.LOWE,
AUTHOR 2 E.D.LAUE
REVDAT 6 25-SEP-19 1E0A 1 COMPND SOURCE REMARK DBREF
REVDAT 6 2 1 SEQADV
REVDAT 5 05-FEB-14 1E0A 1 SOURCE
REVDAT 4 15-MAY-13 1E0A 1 HEADER COMPND SOURCE KEYWDS
REVDAT 4 2 1 AUTHOR JRNL REMARK VERSN
REVDAT 4 3 1 DBREF SEQADV FORMUL HELIX
REVDAT 4 4 1 SHEET ATOM TER HETATM
REVDAT 4 5 1 MASTER
REVDAT 3 24-FEB-09 1E0A 1 VERSN
REVDAT 2 14-SEP-00 1E0A 1 COMPND
REVDAT 1 18-APR-00 1E0A 0
JRNL AUTH A.MORREALE,M.VENKATESAN,H.R.MOTT,D.OWEN,D.NIETLISPACH,
JRNL AUTH 2 P.N.LOWE,E.D.LAUE
JRNL TITL SOLUTION STRUCTURE OF CDC42 BOUND TO THE GTPASE BINDING
JRNL TITL 2 DOMIAN OF PAK
JRNL REF NAT.STRUCT.BIOL. V. 7 384 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 10802735
JRNL DOI 10.1038/75158
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1E0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1290004744.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 5 MM NA2HPO4, 25MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; TRIPLE RESONANCE
REMARK 210 EXPERIMENTS; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA, ANSIG, CNS
REMARK 210 METHOD USED : DISTANCE GEOMETRY OF A
REMARK 210 SUBSTRUCTURE FOLLOWED BY
REMARK 210 CARTESIAN DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: SAMPLES WERE 13C,15N LABELLED CDC42 + UNLABELLED PAK OR
REMARK 210 13C,15N LABELLED PAK + UNLABELLED CDC42
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: 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 400
REMARK 400 COMPOUND
REMARK 400 CHAIN A: ENGINEERED MUTATION GLN61LEU
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 O TYR A 72 H THR A 75 1.60
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 GLN A 2 140.90 69.44
REMARK 500 1 ALA A 13 84.28 53.41
REMARK 500 1 LYS A 16 -74.19 -62.92
REMARK 500 1 LEU A 19 -73.50 -61.26
REMARK 500 1 THR A 24 -86.23 -123.94
REMARK 500 1 ASN A 26 -56.28 79.03
REMARK 500 1 PRO A 29 165.09 -45.82
REMARK 500 1 SER A 30 -76.44 -119.56
REMARK 500 1 PRO A 34 92.71 -43.81
REMARK 500 1 THR A 35 87.64 -51.98
REMARK 500 1 PHE A 37 -68.76 -146.62
REMARK 500 1 ASP A 38 131.48 60.47
REMARK 500 1 PRO A 50 155.95 -46.38
REMARK 500 1 ALA A 59 -66.71 -127.17
REMARK 500 1 LEU A 61 -53.97 170.48
REMARK 500 1 TYR A 72 102.70 46.29
REMARK 500 1 ASP A 76 -165.40 167.97
REMARK 500 1 VAL A 84 -69.92 -109.09
REMARK 500 1 VAL A 85 -73.73 -52.03
REMARK 500 1 SER A 86 106.16 -50.88
REMARK 500 1 LYS A 94 -70.52 -69.61
REMARK 500 1 CYS A 105 74.49 -152.88
REMARK 500 1 GLN A 116 71.40 177.32
REMARK 500 1 ASP A 121 -47.65 174.65
REMARK 500 1 LYS A 135 168.39 69.77
REMARK 500 1 PRO A 136 92.03 -51.27
REMARK 500 1 LYS A 150 108.94 70.59
REMARK 500 1 LYS A 153 139.77 73.87
REMARK 500 1 ALA A 159 -174.05 -52.16
REMARK 500 1 LEU A 160 -64.91 67.72
REMARK 500 1 GLU A 178 81.83 50.51
REMARK 500 1 PRO A 179 102.58 -46.84
REMARK 500 1 PRO A 182 74.00 -65.29
REMARK 500 1 SER B 74 -83.24 -100.06
REMARK 500 1 PHE B 81 124.06 171.41
REMARK 500 1 HIS B 83 95.65 -68.91
REMARK 500 1 THR B 93 50.42 -155.48
REMARK 500 1 LEU B 107 -69.68 -96.20
REMARK 500 1 GLN B 108 -105.10 -80.40
REMARK 500 1 THR B 109 -24.14 159.34
REMARK 500 1 THR B 113 -63.52 68.99
REMARK 500 1 SER B 115 -82.44 60.80
REMARK 500 2 ASP A 11 -152.31 -60.00
REMARK 500 2 LYS A 16 -73.71 -95.91
REMARK 500 2 LEU A 19 -72.86 -55.71
REMARK 500 2 THR A 24 -88.07 -120.63
REMARK 500 2 ASN A 26 51.91 76.64
REMARK 500 2 PHE A 28 168.39 -45.85
REMARK 500 2 SER A 30 -76.25 -107.44
REMARK 500 2 PRO A 34 91.74 -41.58
REMARK 500
REMARK 500 THIS ENTRY HAS 934 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 MG A 186 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GNP A 185 O2G
REMARK 620 2 HOH A 187 O 91.8
REMARK 620 3 THR A 35 OG1 89.9 90.2
REMARK 620 4 HOH A 188 O 81.9 169.8 81.9
REMARK 620 5 THR A 17 OG1 171.7 93.6 96.3 93.5
REMARK 620 6 GNP A 185 O2B 84.4 93.5 173.3 93.8 89.0
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD:
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED. STRANDS 1, 2, 3 AND 4 OF SHEET
REMARK 700 A1 AND A2 ARE IDENTICAL.
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 186
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 185
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 Q61L MUTANT. 7 C-TERMINAL RESIDUES REMOVED
REMARK 999 RESIDUES 73 AND 74 ARE FROM THE EXPRESSION SYSTEM
DBREF 1E0A A 1 184 UNP P60953 CDC42_HUMAN 1 184
DBREF 1E0A B 75 118 UNP P35465 PAK1_RAT 75 118
SEQADV 1E0A LEU A 61 UNP P60953 GLN 61 ENGINEERED MUTATION
SEQADV 1E0A GLY B 73 UNP P35465 EXPRESSION TAG
SEQADV 1E0A SER B 74 UNP P35465 EXPRESSION TAG
SEQRES 1 A 184 MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 184 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 184 LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN
SEQRES 4 A 184 TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR
SEQRES 5 A 184 LEU GLY LEU PHE ASP THR ALA GLY LEU GLU ASP TYR ASP
SEQRES 6 A 184 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 184 LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU
SEQRES 8 A 184 ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS
SEQRES 9 A 184 CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE
SEQRES 10 A 184 ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA
SEQRES 11 A 184 LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU
SEQRES 12 A 184 LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU
SEQRES 13 A 184 CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN VAL PHE
SEQRES 14 A 184 ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO PRO GLU PRO
SEQRES 15 A 184 LYS LYS
SEQRES 1 B 46 GLY SER ILE SER LEU PRO SER ASP PHE GLU HIS THR ILE
SEQRES 2 B 46 HIS VAL GLY PHE ASP ALA VAL THR GLY GLU PHE THR GLY
SEQRES 3 B 46 MET PRO GLU GLN TRP ALA ARG LEU LEU GLN THR SER ASN
SEQRES 4 B 46 ILE THR LYS SER GLU GLN LYS
HET GNP A 185 45
HET MG A 186 1
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 3 GNP C10 H17 N6 O13 P3
FORMUL 4 MG MG 2+
FORMUL 5 HOH *2(H2 O)
HELIX 1 1 LYS A 16 TYR A 23 1 8
HELIX 2 2 TYR A 72 ASP A 76 5 5
HELIX 3 3 SER A 86 VAL A 98 1 13
HELIX 4 4 GLU A 100 CYS A 105 1 6
HELIX 5 5 ASP A 122 ALA A 130 1 9
HELIX 6 6 GLU A 140 LYS A 150 1 11
HELIX 7 7 GLY A 164 GLU A 178 1 15
HELIX 8 8 ALA B 91 GLY B 94 5 4
HELIX 9 9 PRO B 100 LEU B 107 1 8
SHEET 1 AA 4 PHE A 56 THR A 58 0
SHEET 2 AA 4 VAL A 7 VAL A 9 1 O VAL A 8 N THR A 58
SHEET 3 AA 4 PHE A 78 LEU A 79 1 O LEU A 79 N VAL A 9
SHEET 4 AA 4 PHE A 110 LEU A 111 1 N LEU A 111 O PHE A 78
SHEET 1 BA 2 GLY B 88 ASP B 90 0
SHEET 2 BA 2 GLU B 95 THR B 97 -1 O GLU B 95 N ASP B 90
LINK MG MG A 186 O2G GNP A 185 1555 1555 2.39
LINK MG MG A 186 O HOH A 187 1555 1555 2.37
LINK MG MG A 186 OG1 THR A 35 1555 1555 2.40
LINK MG MG A 186 O HOH A 188 1555 1555 2.37
LINK MG MG A 186 OG1 THR A 17 1555 1555 2.38
LINK MG MG A 186 O2B GNP A 185 1555 1555 2.37
SITE 1 AC1 5 THR A 17 THR A 35 GNP A 185 HOH A 187
SITE 2 AC1 5 HOH A 188
SITE 1 AC2 21 ALA A 13 THR A 17 CYS A 18 LEU A 19
SITE 2 AC2 21 ILE A 21 SER A 22 TYR A 23 PHE A 28
SITE 3 AC2 21 PRO A 29 THR A 35 CYS A 81 VAL A 113
SITE 4 AC2 21 THR A 115 GLU A 156 CYS A 157 SER A 158
SITE 5 AC2 21 ALA A 159 GLN A 162 LEU A 165 MG A 186
SITE 6 AC2 21 HOH A 188
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
Complete list - p 25 2 Bytes