Header list of 2gbq.pdb file
Complete list - r 9 2 Bytes
HEADER COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) 23-DEC-96 2GBQ
TITLE SOLUTION NMR STRUCTURE OF THE GRB2 N-TERMINAL SH3 DOMAIN COMPLEXED
TITLE 2 WITH A TEN-RESIDUE PEPTIDE DERIVED FROM SOS DIRECT REFINEMENT AGAINST
TITLE 3 NOES, J-COUPLINGS, AND 1H AND 13C CHEMICAL SHIFTS, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRB2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL SH3 DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SOS-1;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: RESIDUES 1135 - 1144;
COMPND 10 SYNONYM: AC-VPPPVPPRRR-NH2;
COMPND 11 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 STRAIN: BALB/C;
SOURCE 6 CELL_LINE: BL21;
SOURCE 7 CELLULAR_LOCATION: CYTOPLASMIC;
SOURCE 8 GENE: POTENTIAL;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR: PGTX-2T (PHARMACIA);
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: BL21;
SOURCE 15 MOL_ID: 2;
SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 17 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 18 ORGANISM_TAXID: 10090;
SOURCE 19 CELLULAR_LOCATION: CYTOPLASM
KEYWDS COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE), SH3 DOMAIN, COMPLEX (SIGNAL
KEYWDS 2 TRANSDUCTION-PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.WITTEKIND,C.MAPELLI,V.LEE,V.GOLDFARB,M.S.FRIEDRICHS,C.A.MEYERS,
AUTHOR 2 L.MUELLER
REVDAT 3 09-MAR-22 2GBQ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2GBQ 1 VERSN
REVDAT 1 04-SEP-97 2GBQ 0
JRNL AUTH M.WITTEKIND,C.MAPELLI,V.LEE,V.GOLDFARB,M.S.FRIEDRICHS,
JRNL AUTH 2 C.A.MEYERS,L.MUELLER
JRNL TITL SOLUTION STRUCTURE OF THE GRB2 N-TERMINAL SH3 DOMAIN
JRNL TITL 2 COMPLEXED WITH A TEN-RESIDUE PEPTIDE DERIVED FROM SOS:
JRNL TITL 3 DIRECT REFINEMENT AGAINST NOES, J-COUPLINGS AND 1H AND 13C
JRNL TITL 4 CHEMICAL SHIFTS.
JRNL REF J.MOL.BIOL. V. 267 933 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9135122
JRNL DOI 10.1006/JMBI.1996.0886
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.WITTEKIND,C.MAPELLI,B.T.FARMER II,K.L.SUEN,V.GOLDFARB,
REMARK 1 AUTH 2 J.TSAO,T.LAVOIE,M.BARBACID,C.A.MEYERS,L.MUELLER
REMARK 1 TITL ORIENTATION OF PEPTIDE FRAGMENTS FROM SOS PROTEINS BOUND TO
REMARK 1 TITL 2 THE N-TERMINAL SH3 DOMAIN OF GRB2 DETERMINED BY NMR
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 33 13531 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.L.SUEN,X.R.BUSTELO,T.PAWSON,M.BARBACID
REMARK 1 TITL MOLECULAR CLONING OF THE MOUSE GRB2 GENE: DIFFERENTIAL
REMARK 1 TITL 2 INTERACTION OF THE GRB2 ADAPTOR PROTEIN WITH EPIDERMAL
REMARK 1 TITL 3 GROWTH FACTOR AND NERVE GROWTH FACTOR RECEPTORS
REMARK 1 REF MOL.CELL.BIOL. V. 13 5500 1993
REMARK 1 REFN ISSN 0270-7306
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.BOWTELL,P.FU,M.SIMON,P.SENIOR
REMARK 1 TITL IDENTIFICATION OF MURINE HOMOLOGUES OF THE DROSOPHILA SON OF
REMARK 1 TITL 2 SEVENLESS GENE: POTENTIAL ACTIVATORS OF RAS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 6511 1992
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TWO ENSEMBLES WERE CALCULATED. BOTH
REMARK 3 USED THE SAME SET OF NOE/ANGLE/J-COUPLING RESTRAINTS, BUT THEY
REMARK 3 DIFFER IN THAT THE 2ND ENSEMBLE ALSO INCLUDED 1H AND 13C
REMARK 3 CHEMICAL SHIFTS AS RESTRAINTS (SEE PRIMARY REFERENCE FOR DETAILS)
REMARK 3 . RMSD BOND DISTANCES 0.009 +/- 0.0002 ANGSTROMS RMSD BOND ANGLE
REMARK 3 2.70 +/- 0.08 DEGREES BACKBONE RMSD (N, CA, C, O) = 0.38 +/-
REMARK 3 0.11 (SH3 DOMAIN RESIDUES 1 - 26, 36 - 54 AND SOS-E PEPTIDE
REMARK 3 RESIDUES 2 - 7)
REMARK 4
REMARK 4 2GBQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178125.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE JOURNAL ARTICLE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DG, SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -8
REMARK 465 SER A -7
REMARK 465 ARG A -6
REMARK 465 ARG A -5
REMARK 465 ALA A -4
REMARK 465 SER A -3
REMARK 465 VAL A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 HIS A 58
REMARK 465 PRO A 59
REMARK 465 GLU A 60
REMARK 465 PHE A 61
REMARK 465 ILE A 62
REMARK 465 VAL A 63
REMARK 465 THR A 64
REMARK 465 ASP A 65
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 SER A 18 CB SER A 18 OG 0.086
REMARK 500 8 SER A 18 CB SER A 18 OG 0.087
REMARK 500 13 SER A 18 CB SER A 18 OG 0.088
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 LEU A 41 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 2 LEU A 41 CB - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 3 LEU A 41 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 4 LEU A 41 CB - CA - C ANGL. DEV. = -11.4 DEGREES
REMARK 500 7 LEU A 41 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 8 LEU A 41 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 9 LEU A 41 CB - CA - C ANGL. DEV. = -12.0 DEGREES
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 ARG A 21 100.96 -46.05
REMARK 500 1 ASN A 29 169.99 78.26
REMARK 500 1 CYS A 32 -42.94 77.73
REMARK 500 1 GLN A 34 60.72 -106.46
REMARK 500 1 ASN A 35 -15.46 175.50
REMARK 500 1 LYS A 56 83.53 -154.52
REMARK 500 1 PRO B 3 159.83 -47.79
REMARK 500 1 ARG B 9 51.88 -160.29
REMARK 500 2 ARG A 21 102.41 -45.94
REMARK 500 2 ASN A 29 170.48 86.88
REMARK 500 2 CYS A 32 7.86 -60.57
REMARK 500 2 GLN A 34 58.87 27.39
REMARK 500 2 ASN A 35 -12.92 -168.15
REMARK 500 2 PRO B 2 113.21 10.25
REMARK 500 2 PRO B 3 158.47 -40.31
REMARK 500 2 ARG B 9 84.27 162.94
REMARK 500 3 GLN A 34 64.84 -109.22
REMARK 500 3 ASN A 35 -23.29 -179.11
REMARK 500 3 LYS A 56 84.72 -153.70
REMARK 500 3 PRO B 3 155.70 -42.00
REMARK 500 3 ARG B 9 72.61 -153.51
REMARK 500 4 ARG A 21 100.89 -45.90
REMARK 500 4 LEU A 28 -69.55 -93.52
REMARK 500 4 GLU A 30 57.38 -144.53
REMARK 500 4 GLU A 31 49.08 -154.40
REMARK 500 4 CYS A 32 -50.27 -141.14
REMARK 500 4 GLN A 34 41.56 -107.31
REMARK 500 4 ASN A 35 -30.35 -158.22
REMARK 500 4 PRO B 3 157.77 -45.15
REMARK 500 4 ARG B 9 30.53 72.81
REMARK 500 5 ARG A 21 101.30 -46.18
REMARK 500 5 GLU A 31 -139.93 -102.34
REMARK 500 5 GLN A 34 60.61 -105.94
REMARK 500 5 ASN A 35 -22.74 -169.20
REMARK 500 5 MET A 55 -79.68 -84.48
REMARK 500 5 LYS A 56 98.19 65.81
REMARK 500 5 PRO B 3 162.14 -43.10
REMARK 500 5 ARG B 9 85.32 133.78
REMARK 500 6 ARG A 21 54.95 3.78
REMARK 500 6 GLU A 31 34.02 -172.58
REMARK 500 6 CYS A 32 -73.93 -112.34
REMARK 500 6 ASN A 35 -22.98 -173.57
REMARK 500 6 PRO B 3 164.14 -42.76
REMARK 500 6 ARG B 9 53.74 -147.45
REMARK 500 7 ALA A 13 88.80 59.63
REMARK 500 7 ASP A 15 19.94 117.09
REMARK 500 7 ARG A 21 95.31 3.44
REMARK 500 7 GLU A 30 106.63 -160.33
REMARK 500 7 GLU A 31 38.54 -170.82
REMARK 500 7 CYS A 32 -78.72 -139.90
REMARK 500
REMARK 500 THIS ENTRY HAS 114 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 11
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GBQ RELATED DB: PDB
DBREF 2GBQ A 1 61 UNP Q60631 GRB2_MOUSE 1 61
DBREF 2GBQ B 1 10 UNP Q62245 SOS1_MOUSE 1135 1144
SEQADV 2GBQ GLU A 60 UNP Q60631 TRP 60 CONFLICT
SEQRES 1 A 74 GLY SER ARG ARG ALA SER VAL GLY SER MET GLU ALA ILE
SEQRES 2 A 74 ALA LYS TYR ASP PHE LYS ALA THR ALA ASP ASP GLU LEU
SEQRES 3 A 74 SER PHE LYS ARG GLY ASP ILE LEU LYS VAL LEU ASN GLU
SEQRES 4 A 74 GLU CYS ASP GLN ASN TRP TYR LYS ALA GLU LEU ASN GLY
SEQRES 5 A 74 LYS ASP GLY PHE ILE PRO LYS ASN TYR ILE GLU MET LYS
SEQRES 6 A 74 PRO HIS PRO GLU PHE ILE VAL THR ASP
SEQRES 1 B 12 ACE VAL PRO PRO PRO VAL PRO PRO ARG ARG ARG NH2
HET ACE B 0 6
HET NH2 B 11 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 2 ACE C2 H4 O
FORMUL 2 NH2 H2 N
HELIX 1 1 LYS A 50 TYR A 52 5 3
SHEET 1 A 3 ILE A 24 LYS A 26 0
SHEET 2 A 3 GLU A 2 ALA A 5 -1 N ALA A 3 O LEU A 25
SHEET 3 A 3 ILE A 53 LYS A 56 -1 N LYS A 56 O GLU A 2
SHEET 1 B 2 TRP A 36 LEU A 41 0
SHEET 2 B 2 LYS A 44 PRO A 49 -1 N ILE A 48 O TYR A 37
LINK C ACE B 0 N VAL B 1 1555 1555 1.36
LINK C ARG B 10 N NH2 B 11 1555 1555 1.34
SITE 1 AC2 2 ARG B 9 ARG B 10
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 - r 9 2 Bytes