Header list of 1k1z.pdb file
Complete list - 10 20 Bytes
HEADER SIGNALING PROTEIN 26-SEP-01 1K1Z
TITLE SOLUTION STRUCTURE OF N-TERMINAL SH3 DOMAIN MUTANT(P33G) OF MURINE VAV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VAV;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL SH3 DOMAIN;
COMPND 5 SYNONYM: VAV PROTO-ONCOGENE;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PHT-1
KEYWDS SH3, PROTO-ONCOGENE, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR K.OGURA,K.NAGATA,M.HORIUCHI,E.EBISUI,T.HASUDA,S.YUZAWA,M.NISHIDA,
AUTHOR 2 H.HATANAKA,F.INAGAKI
REVDAT 4 10-NOV-21 1K1Z 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1K1Z 1 VERSN
REVDAT 2 24-JUN-03 1K1Z 1 JRNL
REVDAT 1 10-OCT-01 1K1Z 0
JRNL AUTH K.OGURA,K.NAGATA,M.HORIUCHI,E.EBISUI,T.HASUDA,S.YUZAWA,
JRNL AUTH 2 M.NISHIDA,H.HATANAKA,F.INAGAKI
JRNL TITL SOLUTION STRUCTURE OF N-TERMINAL SH3 DOMAIN OF VAV AND THE
JRNL TITL 2 RECOGNITION SITE FOR GRB2 C-TERMINAL SH3 DOMAIN
JRNL REF J.BIOMOL.NMR V. 22 37 2002
JRNL REFN ISSN 0925-2738
JRNL PMID 11885979
JRNL DOI 10.1023/A:1013868731495
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.0, ARIA 1.0
REMARK 3 AUTHORS : NILGES (ARIA), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K1Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014459.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM PROTEIN U-15N,13C; 10MM
REMARK 210 PHOSPHATE BUFFER K; 10MM DTT-D
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: 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 LYS A 5 -17.18 -141.89
REMARK 500 PRO A 39 92.39 -58.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K1Z A 1 78 UNP P27870 VAV_MOUSE 583 660
SEQADV 1K1Z GLY A 33 UNP P27870 PRO 615 ENGINEERED MUTATION
SEQRES 1 A 78 ARG ALA GLN ASP LYS LYS ARG ASN GLU LEU GLY LEU PRO
SEQRES 2 A 78 LYS MET GLU VAL PHE GLN GLU TYR TYR GLY ILE PRO PRO
SEQRES 3 A 78 PRO PRO GLY ALA PHE GLY GLY PHE LEU ARG LEU ASN PRO
SEQRES 4 A 78 GLY ASP ILE VAL GLU LEU THR LYS ALA GLU ALA GLU HIS
SEQRES 5 A 78 ASN TRP TRP GLU GLY ARG ASN THR ALA THR ASN GLU VAL
SEQRES 6 A 78 GLY TRP PHE PRO CYS ASN ARG VAL HIS PRO TYR VAL HIS
SHEET 1 A 5 GLU A 64 PHE A 68 0
SHEET 2 A 5 TRP A 55 ASN A 59 -1 N TRP A 55 O PHE A 68
SHEET 3 A 5 ILE A 42 LYS A 47 -1 N GLU A 44 O ARG A 58
SHEET 4 A 5 MET A 15 VAL A 17 -1 N MET A 15 O VAL A 43
SHEET 5 A 5 VAL A 73 PRO A 75 -1 O HIS A 74 N GLU A 16
CISPEP 1 ILE A 24 PRO A 25 0 0.17
CRYST1 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
Complete list - 10 20 Bytes