Header list of 1h92.pdb file
Complete list - r 25 2 Bytes
HEADER TRANSFERASE 22-FEB-01 1H92 TITLE SH3 DOMAIN OF HUMAN LCK TYROSINE KINASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH3 DOMAIN RESIDUES 57-119; COMPND 5 SYNONYM: TYROSINE-PROTEIN KINASE LCK, P56-LCK; COMPND 6 ENGINEERED: 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: INTRACELLULAR; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-2 KEYWDS TRANSFERASE, SH3 DOMAIN, TYROSINE KINASE, SIGNAL KEYWDS 2 TRANSDUCTION, LCK EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR K.SCHWEIMER,S.HOFFMANN,U.FRIEDRICH,B.BIESINGER,P.ROESCH, AUTHOR 2 H.STICHT REVDAT 3 24-FEB-09 1H92 1 VERSN REVDAT 2 12-JUL-05 1H92 1 JRNL REVDAT 1 22-OCT-01 1H92 0 JRNL AUTH K.SCHWEIMER,S.HOFFMANN,F.BAUER,U.FRIEDRICH, JRNL AUTH 2 C.KARDINAL,S.M.FELLER,B.BIESINGER,H.STICHT JRNL TITL STRUCTURAL INVESTIGATION OF THE BINDING OF A JRNL TITL 2 HERPESVIRAL PROTEIN TO THE SH3 DOMAIN OF TYROSINE JRNL TITL 3 KINASE LCK JRNL REF BIOCHEMISTRY V. 41 5120 2002 JRNL REFN ISSN 0006-2960 JRNL PMID 11955060 JRNL DOI 10.1021/BI015986J REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN REMARK 3 THE JRNL CITATION ABOVE. REMARK 4 REMARK 4 1H92 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-FEB-01. REMARK 100 THE PDBE ID CODE IS EBI-5908. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.4 REMARK 210 IONIC STRENGTH : 150 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-EDITED NOESY, REMARK 210 3D 13C-EDITED NOESY, REMARK 210 2D 15N-FILTERED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW, XPLOR REMARK 210 METHOD USED : AB INITIO SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE REMARK 210 NMR SPECTROSCOPY ON 13C, 15N LABELED LCK-SH3 DOMAIN 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 ALA A 11 - H GLY A 28 1.56 REMARK 500 H LEU A 12 - O PHE A 58 1.57 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 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 HIS A 19 -155.35 -128.23 REMARK 500 1 PHE A 25 171.11 -45.57 REMARK 500 2 PHE A 25 172.19 -45.32 REMARK 500 3 PHE A 25 172.50 -48.46 REMARK 500 4 PHE A 25 171.74 -50.26 REMARK 500 4 GLN A 36 58.60 -142.09 REMARK 500 4 PRO A 55 159.35 -47.16 REMARK 500 5 PHE A 25 169.59 -44.78 REMARK 500 6 PHE A 25 173.53 -50.14 REMARK 500 7 HIS A 19 -158.25 -141.02 REMARK 500 7 PHE A 25 171.21 -49.91 REMARK 500 8 PHE A 25 168.72 -48.28 REMARK 500 9 PRO A 17 91.53 -59.96 REMARK 500 9 PHE A 25 174.42 -53.36 REMARK 500 10 PHE A 25 175.78 -48.74 REMARK 500 11 HIS A 13 -158.95 -149.35 REMARK 500 11 PHE A 25 171.60 -50.80 REMARK 500 12 PHE A 25 171.88 -47.36 REMARK 500 13 PHE A 25 170.21 -48.10 REMARK 500 14 PHE A 25 174.44 -50.43 REMARK 500 15 GLU A 16 75.28 -110.11 REMARK 500 15 HIS A 19 -158.26 -140.55 REMARK 500 15 PHE A 25 172.71 -54.20 REMARK 500 16 PRO A 17 98.91 -62.99 REMARK 500 16 PHE A 25 171.35 -52.94 REMARK 500 16 GLU A 35 125.49 -172.72 REMARK 500 16 GLN A 36 62.88 -101.87 REMARK 500 17 LEU A 4 -85.34 55.86 REMARK 500 17 PHE A 25 176.33 -50.76 REMARK 500 18 PHE A 25 171.62 -46.64 REMARK 500 19 PHE A 25 174.55 -49.29 REMARK 500 19 ALA A 62 154.97 -43.45 REMARK 500 20 PHE A 25 171.13 -45.31 REMARK 500 20 GLN A 36 57.80 -151.09 REMARK 500 21 PHE A 25 176.57 -53.39 REMARK 500 22 GLU A 16 79.48 -106.90 REMARK 500 22 PRO A 17 109.62 -47.45 REMARK 500 22 PHE A 25 175.99 -54.76 REMARK 500 23 PRO A 17 104.55 -48.55 REMARK 500 23 PHE A 25 170.60 -47.34 REMARK 500 23 GLN A 36 58.10 -142.25 REMARK 500 23 PRO A 55 167.41 -46.37 REMARK 500 23 ALA A 62 -145.73 49.62 REMARK 500 24 PHE A 25 174.13 -53.67 REMARK 500 25 GLU A 16 73.87 -114.07 REMARK 500 25 PHE A 25 169.45 -47.07 REMARK 500 25 ALA A 60 -41.28 -160.26 REMARK 500 25 ALA A 62 25.13 49.18 REMARK 500 26 HIS A 19 -159.34 -129.13 REMARK 500 26 PHE A 25 173.43 -48.43 REMARK 500 27 PHE A 25 173.73 -53.12 REMARK 500 28 PHE A 25 175.44 -52.61 REMARK 500 29 GLU A 16 77.83 -110.45 REMARK 500 29 PRO A 17 98.99 -41.52 REMARK 500 29 PHE A 25 174.50 -54.13 REMARK 500 30 PRO A 17 96.20 -44.36 REMARK 500 30 PHE A 25 172.35 -48.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 32 0.11 SIDE CHAIN REMARK 500 2 ARG A 32 0.10 SIDE CHAIN REMARK 500 3 ARG A 32 0.23 SIDE CHAIN REMARK 500 4 ARG A 32 0.31 SIDE CHAIN REMARK 500 5 ARG A 32 0.15 SIDE CHAIN REMARK 500 6 ARG A 32 0.24 SIDE CHAIN REMARK 500 7 ARG A 32 0.29 SIDE CHAIN REMARK 500 8 ARG A 32 0.22 SIDE CHAIN REMARK 500 9 ARG A 32 0.20 SIDE CHAIN REMARK 500 10 ARG A 32 0.31 SIDE CHAIN REMARK 500 11 ARG A 32 0.32 SIDE CHAIN REMARK 500 12 ARG A 32 0.17 SIDE CHAIN REMARK 500 13 ARG A 32 0.30 SIDE CHAIN REMARK 500 14 ARG A 32 0.31 SIDE CHAIN REMARK 500 15 ARG A 32 0.32 SIDE CHAIN REMARK 500 16 ARG A 32 0.28 SIDE CHAIN REMARK 500 17 ARG A 32 0.26 SIDE CHAIN REMARK 500 18 ARG A 32 0.32 SIDE CHAIN REMARK 500 20 ARG A 32 0.31 SIDE CHAIN REMARK 500 21 ARG A 32 0.18 SIDE CHAIN REMARK 500 22 ARG A 32 0.17 SIDE CHAIN REMARK 500 23 ARG A 32 0.32 SIDE CHAIN REMARK 500 24 ARG A 32 0.13 SIDE CHAIN REMARK 500 25 ARG A 32 0.15 SIDE CHAIN REMARK 500 26 ARG A 32 0.28 SIDE CHAIN REMARK 500 27 ARG A 32 0.32 SIDE CHAIN REMARK 500 28 ARG A 32 0.11 SIDE CHAIN REMARK 500 30 ARG A 32 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FBZ RELATED DB: PDB REMARK 900 STRUCTURE-BASED DESIGN OF A NOVEL, REMARK 900 OSTEOCLAST-SELECTIVE,NONPEPTIDE SRC SH2 REMARK 900 INHIBITOR WITH IN VIVO ANTI-RESORPTIVEACTIVITY REMARK 900 RELATED ID: 1LCJ RELATED DB: PDB REMARK 900 SH2 (SRC HOMOLOGY-2) DOMAIN OF HUMAN P56- REMARK 900 LCK TYROSINE KINASE COMPLEXED WITH THE 11 REMARK 900 RESIDUE PHOSPHOTYROSYL PEPTIDE EPQPYEEIPIYL REMARK 900 RELATED ID: 1LCK RELATED DB: PDB REMARK 900 SH3-SH2 DOMAIN FRAGMENT OF HUMAN P56-LCK REMARK 900 TYROSINE KINASE COMPLEXED WITH THE 10 REMARK 900 RESIDUE SYNTHETIC PHOSPHOTYROSYL PEPTIDE REMARK 900 TEGQPYQPQPA REMARK 900 RELATED ID: 1QPC RELATED DB: PDB REMARK 900 STRUCTURAL ANALYSIS OF THE LYMPHOCYTE-SPECIFIC REMARK 900 KINASE LCK IN COMPLEX WITH NON-SELECTIVE REMARK 900 AND SRC FAMILY SELECTIVE KINASE INHIBITORS REMARK 900 RELATED ID: 1QPD RELATED DB: PDB REMARK 900 STRUCTURAL ANALYSIS OF THE LYMPHOCYTE-SPECIFIC REMARK 900 KINASE LCK IN COMPLEX WITH NON-SELECTIVE REMARK 900 AND SRC FAMILY SELECTIVE KINASE INHIBITORS REMARK 900 RELATED ID: 1QPE RELATED DB: PDB REMARK 900 STRUCTURAL ANALYSIS OF THE LYMPHOCYTE-SPECIFIC REMARK 900 KINASE LCK IN COMPLEX WITH NON-SELECTIVE REMARK 900 AND SRC FAMILY SELECTIVE KINASE INHIBITORS REMARK 900 RELATED ID: 1QPJ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE LYMPHOCYTE-SPECIFIC REMARK 900 KINASE LCK IN COMPLEX WITH STAUROSPORINE. REMARK 900 RELATED ID: 3LCK RELATED DB: PDB REMARK 900 THE KINASE DOMAIN OF HUMAN LYMPHOCYTE KINASE REMARK 900 (LCK), ACTIVATED FORM (AUTO-PHOSPHORYLATED REMARK 900 ON TYR394) REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE ALA TO GLY MUTATION AROSE FROM THE EXPRESSION SYSTEM REMARK 999 USED IN WHICH THE N-TERMINAL GST-FUSION PARTNER WAS REMARK 999 REMOVED BY THROMBIN CLEAVAGE. DBREF 1H92 A 1 63 UNP P06239 LCK_HUMAN 57 119 SEQADV 1H92 GLY A 1 UNP P06239 ALA 57 CONFLICT SEQRES 1 A 63 GLY SER PRO LEU GLN ASP ASN LEU VAL ILE ALA LEU HIS SEQRES 2 A 63 SER TYR GLU PRO SER HIS ASP GLY ASP LEU GLY PHE GLU SEQRES 3 A 63 LYS GLY GLU GLN LEU ARG ILE LEU GLU GLN SER GLY GLU SEQRES 4 A 63 TRP TRP LYS ALA GLN SER LEU THR THR GLY GLN GLU GLY SEQRES 5 A 63 PHE ILE PRO PHE ASN PHE VAL ALA LYS ALA ASN SHEET 1 AA 5 GLU A 51 PRO A 55 0 SHEET 2 AA 5 TRP A 40 SER A 45 -1 O TRP A 41 N ILE A 54 SHEET 3 AA 5 GLN A 30 ILE A 33 -1 O ARG A 32 N GLN A 44 SHEET 4 AA 5 LEU A 8 ALA A 11 -1 O VAL A 9 N LEU A 31 SHEET 5 AA 5 VAL A 59 LYS A 61 -1 O ALA A 60 N ILE A 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 25 2 Bytes