Header list of 3hck.pdb file
Complete list - r 16 2 Bytes
HEADER TRANSFERASE 31-MAR-97 3HCK
TITLE NMR ENSEMBLE OF THE UNCOMPLEXED HUMAN HCK SH2 DOMAIN, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HCK SH2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2, RESIDUES 119 - 224 OF HUMAN HCK;
COMPND 5 EC: 2.7.10.2;
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 CELL_LINE: BL21;
SOURCE 6 GENE: RESIDUES E119-K224 OF HUMAN HC;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-14B;
SOURCE 11 EXPRESSION_SYSTEM_GENE: RESIDUES E119-K224 OF HUMAN HCK
KEYWDS HCK, SH2, TYROSINE KINASE, SIGNAL TRANSDUCTION, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.ZHANG,T.E.SMITHGALL,W.H.GMEINER
REVDAT 4 16-MAR-22 3HCK 1 REMARK
REVDAT 3 24-FEB-09 3HCK 1 VERSN
REVDAT 2 03-JAN-06 3HCK 1 HELIX
REVDAT 1 15-OCT-97 3HCK 0
JRNL AUTH W.ZHANG,T.E.SMITHGALL,W.H.GMEINER
JRNL TITL SEQUENTIAL ASSIGNMENT AND SECONDARY STRUCTURE DETERMINATION
JRNL TITL 2 FOR THE SRC HOMOLOGY 2 DOMAIN OF HEMATOPOIETIC CELLULAR
JRNL TITL 3 KINASE.
JRNL REF FEBS LETT. V. 406 131 1997
JRNL REFN ISSN 0014-5793
JRNL PMID 9109402
JRNL DOI 10.1016/S0014-5793(97)00255-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,MUMENTHALER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING IN TORSION ANGLE
REMARK 3 SPACE
REMARK 4
REMARK 4 3HCK 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_1000178997.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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: 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 GLU A 2 138.97 178.61
REMARK 500 1 GLU A 5 51.79 -119.16
REMARK 500 1 LYS A 9 -176.38 -61.45
REMARK 500 1 LEU A 27 129.64 -39.90
REMARK 500 1 LYS A 39 151.29 -48.27
REMARK 500 1 ARG A 52 -62.93 -101.76
REMARK 500 1 ARG A 75 -68.85 -137.85
REMARK 500 1 SER A 100 -77.36 -108.44
REMARK 500 1 CYS A 103 156.90 -46.14
REMARK 500 1 SER A 105 79.97 -170.10
REMARK 500 2 GLU A 5 56.27 -110.22
REMARK 500 2 ARG A 52 -66.76 -93.94
REMARK 500 2 ARG A 75 -55.73 -138.44
REMARK 500 2 SER A 100 -76.25 -96.67
REMARK 500 3 GLU A 2 104.77 55.17
REMARK 500 3 GLU A 5 58.21 -119.97
REMARK 500 3 LYS A 9 -176.69 -62.00
REMARK 500 3 THR A 37 -87.55 -88.82
REMARK 500 3 ASP A 66 32.54 -96.14
REMARK 500 3 ASN A 67 -44.85 -159.46
REMARK 500 3 ARG A 75 -61.77 -138.59
REMARK 500 3 LEU A 95 -177.38 -62.94
REMARK 500 3 SER A 100 -77.11 -101.21
REMARK 500 3 CYS A 103 152.94 -43.11
REMARK 500 4 GLU A 2 113.58 -178.65
REMARK 500 4 GLU A 4 103.40 -172.64
REMARK 500 4 LYS A 9 -172.81 -60.58
REMARK 500 4 ALA A 22 160.34 -43.41
REMARK 500 4 ARG A 75 -63.67 -137.83
REMARK 500 4 SER A 100 -76.03 -90.95
REMARK 500 5 GLU A 5 50.81 -119.92
REMARK 500 5 THR A 37 -66.70 -94.53
REMARK 500 5 ARG A 52 -61.64 -97.83
REMARK 500 5 ARG A 75 -58.60 -134.79
REMARK 500 5 SER A 100 -76.88 -111.84
REMARK 500 5 CYS A 103 151.58 -47.27
REMARK 500 6 GLU A 2 108.42 161.68
REMARK 500 6 GLU A 5 52.15 -108.91
REMARK 500 6 LYS A 9 -176.94 -66.53
REMARK 500 6 LYS A 39 152.57 -49.28
REMARK 500 6 ARG A 52 -60.26 -102.17
REMARK 500 6 ARG A 75 -61.95 -137.59
REMARK 500 6 SER A 100 -78.52 -97.31
REMARK 500 6 CYS A 103 155.13 -43.61
REMARK 500 6 SER A 105 100.39 -170.36
REMARK 500 7 GLU A 5 50.79 -119.58
REMARK 500 7 ARG A 52 -61.29 -98.94
REMARK 500 7 ARG A 75 -66.77 -137.59
REMARK 500 7 SER A 100 -77.55 -97.27
REMARK 500 7 CYS A 103 154.28 -42.29
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3HCK A 2 107 UNP P08631 HCK_HUMAN 140 245
SEQRES 1 A 107 MET GLU THR GLU GLU TRP PHE PHE LYS GLY ILE SER ARG
SEQRES 2 A 107 LYS ASP ALA GLU ARG GLN LEU LEU ALA PRO GLY ASN MET
SEQRES 3 A 107 LEU GLY SER PHE MET ILE ARG ASP SER GLU THR THR LYS
SEQRES 4 A 107 GLY SER TYR SER LEU SER VAL ARG ASP TYR ASP PRO ARG
SEQRES 5 A 107 GLN GLY ASP THR VAL LYS HIS TYR LYS ILE ARG THR LEU
SEQRES 6 A 107 ASP ASN GLY GLY PHE TYR ILE SER PRO ARG SER THR PHE
SEQRES 7 A 107 SER THR LEU GLN GLU LEU VAL ASP HIS TYR LYS LYS GLY
SEQRES 8 A 107 ASN ASP GLY LEU CYS GLN LYS LEU SER VAL PRO CYS MET
SEQRES 9 A 107 SER SER LYS
HELIX 1 1 ARG A 13 LEU A 21 1 9
HELIX 2 2 LEU A 81 GLY A 91 1 11
SHEET 1 A 3 PHE A 30 ASP A 34 0
SHEET 2 A 3 TYR A 42 TYR A 49 -1 N SER A 45 O MET A 31
SHEET 3 A 3 ASP A 55 ILE A 62 -1 N ILE A 62 O TYR A 42
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 16 2 Bytes