Header list of 1m3b.pdb file
Complete list - t 27 2 Bytes
HEADER PROTEIN BINDING 27-JUN-02 1M3B
TITLE SOLUTION STRUCTURE OF A CIRCULAR FORM OF THE N-TERMINAL SH3 DOMAIN
TITLE 2 (A134C, E135G, R191G MUTANT) FROM ONCOGENE PROTEIN C-CRK.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE C-CRK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL SH3 DOMAIN (RESIDUES 134-191);
COMPND 5 SYNONYM: P38, ADAPTER MOLECULE CRK;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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: CRK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS SH3, SH3 DOMAIN, CIRCULAR PROTEIN, CYCLIZED PROTEIN, ADAPTOR PROTEIN,
KEYWDS 2 PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.H.SCHUMANN,R.VARADAN,P.P.TAYAKUNIYIL,J.B.HALL,J.A.CAMARERO,
AUTHOR 2 D.FUSHMAN
REVDAT 3 27-OCT-21 1M3B 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1M3B 1 VERSN
REVDAT 1 05-AUG-03 1M3B 0
JRNL AUTH F.H.SCHUMANN,R.VARADAN,P.P.TAYAKUNIYIL,J.B.HALL,
JRNL AUTH 2 J.A.CAMARERO,D.FUSHMAN
JRNL TITL CHANGING PROTEIN BACKBONE TOPOLOGY: STRUCTURAL AND DYNAMIC
JRNL TITL 2 CONSEQUENCES OF THE BACKBONE CYCLIZATION IN SH3 DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.CAMARERO,D.FUSHMAN,S.SATO,I.GIRIAT,D.COWBURN,
REMARK 1 AUTH 2 D.P.RALEIGH,T.W.MUIR
REMARK 1 TITL RESCUING A DESTABILIZED PROTEIN FOLD THROUGH BACKBONE
REMARK 1 TITL 2 CYCLIZATION
REMARK 1 REF J.MOL.BIOL. V. 308 1045 2001
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2001.4631
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6,3.0, DYANA
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, WUETHRICH (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1151
REMARK 3 RESTRAINTS, 1054 ARE NOE-DERIVED DISTANCE CONTRAINTS, 25
REMARK 3 DIHEDRAL ANGLE CONSTRAINTS, AND 72 DISTANCE RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS. STRUCTURES WERE CALCULATED USING PROGRAM DYANA.
REMARK 3 NO FURTHER REFINEMENT WAS PERFORMED.
REMARK 4
REMARK 4 1M3B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016544.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 307
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM SH3 NA, 20MM SODIUM
REMARK 210 PHOSPHATE, 20 MM DTT-D10, 100 MM
REMARK 210 NACL, 0.1% (W/V) NAN3; 1MM SH3 U-
REMARK 210 15N, 20MM SODIUM PHOSPHATE, 20
REMARK 210 MM DTT-D10, 100 MM NACL, 0.1% (W/
REMARK 210 V) NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY; 2D
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.1.3, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING COMBINED
REMARK 210 WITH TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES COMBINED WITH 2D 1H-15N HSQC DATA.
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
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 ASN A 146 60.66 -159.47
REMARK 500 1 GLU A 148 39.16 -86.63
REMARK 500 1 GLU A 149 -39.73 -144.49
REMARK 500 1 GLN A 168 -49.93 -155.40
REMARK 500 1 ASP A 174 176.69 -57.41
REMARK 500 2 ASN A 146 48.20 176.38
REMARK 500 2 GLU A 148 45.87 -81.64
REMARK 500 2 GLU A 149 -37.63 -160.41
REMARK 500 2 GLN A 168 -60.89 -171.67
REMARK 500 2 ASP A 174 171.07 -55.02
REMARK 500 2 SER A 175 29.93 -77.94
REMARK 500 3 PHE A 141 135.14 -170.62
REMARK 500 3 ASN A 146 -58.64 -173.70
REMARK 500 3 ASP A 147 123.91 166.09
REMARK 500 3 GLN A 168 -66.52 170.15
REMARK 500 3 SER A 175 31.61 -80.59
REMARK 500 4 PHE A 141 118.45 -165.20
REMARK 500 4 ASN A 146 -36.36 178.03
REMARK 500 4 GLU A 148 31.71 -87.06
REMARK 500 4 LYS A 155 106.77 -47.16
REMARK 500 4 GLN A 168 -51.95 79.43
REMARK 500 4 TYR A 190 75.34 -111.18
REMARK 500 5 TYR A 136 -144.83 -144.45
REMARK 500 5 LEU A 140 40.11 -99.51
REMARK 500 5 ASN A 146 74.55 -179.05
REMARK 500 5 GLU A 148 43.18 -86.14
REMARK 500 5 GLU A 149 -41.00 -154.83
REMARK 500 5 GLU A 166 176.67 -51.61
REMARK 500 5 GLN A 168 -56.71 -175.84
REMARK 500 5 ASP A 174 173.43 -54.39
REMARK 500 6 LEU A 140 42.17 -106.12
REMARK 500 6 ASN A 146 -45.24 -174.34
REMARK 500 6 GLU A 148 39.34 -86.02
REMARK 500 6 ARG A 162 -64.87 -101.24
REMARK 500 6 LYS A 164 100.14 84.78
REMARK 500 6 GLU A 166 -145.73 30.99
REMARK 500 6 GLU A 167 44.96 -165.74
REMARK 500 6 GLN A 168 -60.61 -175.23
REMARK 500 6 ASP A 174 172.55 -57.33
REMARK 500 6 TYR A 186 40.58 -84.99
REMARK 500 7 LEU A 140 47.45 -107.77
REMARK 500 7 PHE A 141 134.40 178.12
REMARK 500 7 ASN A 146 43.55 178.57
REMARK 500 7 ASP A 147 174.22 54.72
REMARK 500 7 GLU A 149 -34.95 178.60
REMARK 500 7 ASP A 150 124.83 167.81
REMARK 500 7 GLN A 168 -52.45 76.27
REMARK 500 7 ASP A 174 173.78 -56.70
REMARK 500 7 TYR A 186 33.74 -91.55
REMARK 500 8 LEU A 140 41.63 -97.86
REMARK 500
REMARK 500 THIS ENTRY HAS 151 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M30 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF N-TERMINAL SH3 DOMAIN FROM ONCOGENE PROTEIN C-
REMARK 900 CRK
REMARK 900 RELATED ID: 1M3A RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A CIRCULAR FORM OF THE TRUNCATED N-TERMINAL
REMARK 900 SH3 DOMAIN FROM ONCOGENE PROTEIN C-CRK.
REMARK 900 RELATED ID: 1M3C RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A CIRCULAR FORM OF THE N-TERMINAL SH3 DOMAIN
REMARK 900 FROM ONCOGENE PROTEIN C-CRK
DBREF 1M3B A 134 191 UNP Q64010 CRK_MOUSE 134 191
SEQADV 1M3B CYS A 134 UNP Q64010 ALA 134 ENGINEERED MUTATION
SEQADV 1M3B GLY A 135 UNP Q64010 GLU 135 ENGINEERED MUTATION
SEQADV 1M3B GLY A 191 UNP Q64010 ARG 191 ENGINEERED MUTATION
SEQRES 1 A 58 CYS GLY TYR VAL ARG ALA LEU PHE ASP PHE ASN GLY ASN
SEQRES 2 A 58 ASP GLU GLU ASP LEU PRO PHE LYS LYS GLY ASP ILE LEU
SEQRES 3 A 58 ARG ILE ARG ASP LYS PRO GLU GLU GLN TRP TRP ASN ALA
SEQRES 4 A 58 GLU ASP SER GLU GLY LYS ARG GLY MET ILE PRO VAL PRO
SEQRES 5 A 58 TYR VAL GLU LYS TYR GLY
SHEET 1 A 5 ARG A 179 PRO A 183 0
SHEET 2 A 5 TRP A 169 ASP A 174 -1 N TRP A 170 O ILE A 182
SHEET 3 A 5 LYS A 155 ASP A 163 -1 N ASP A 163 O ASN A 171
SHEET 4 A 5 TYR A 136 LEU A 140 -1 N VAL A 137 O LEU A 159
SHEET 5 A 5 VAL A 187 GLY A 191 -1 O GLY A 191 N TYR A 136
LINK N CYS A 134 C GLY A 191 1555 1555 1.49
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 - t 27 2 Bytes