Header list of 1rja.pdb file
Complete list - r 25 2 Bytes
HEADER TRANSFERASE 18-NOV-03 1RJA
TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE NONRECEPTOR TYROSINE
TITLE 2 KINASE PTK6/BRK SH2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE 6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: BREAST TUMOR KINASE, TYROSINE-PROTEIN KINASE BRK, PTK6/BRK;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PGEX 4T-3
KEYWDS HUMAN PROTEIN TYROSINE KINASE-6 (PTK6/BRK), SRC HOMOLOGY 2(SH2)
KEYWDS 2 DOMAIN, SOLUTION STRUCTURE, BACKBONE DYNAMICS, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR E.HONG,J.SHIN,W.LEE
REVDAT 3 10-AUG-11 1RJA 1 SOURCE VERSN
REVDAT 2 24-FEB-09 1RJA 1 VERSN
REVDAT 1 20-JUL-04 1RJA 0
JRNL AUTH E.HONG,J.SHIN,H.I.KIM,S.T.LEE,W.LEE
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE NON-RECEPTOR
JRNL TITL 2 PROTEIN-TYROSINE KINASE-6 SRC HOMOLOGY 2 DOMAIN
JRNL REF J.BIOL.CHEM. V. 279 29700 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15056653
JRNL DOI 10.1074/JBC.M313185200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.HONG,J.SHIN,E.BANG,M.H.KIM,S.T.LEE,W.LEE
REMARK 1 TITL LETTER TO THE EDITOR: COMPLETE SEQUENCE-SPECIFIC 1H, 13C AND
REMARK 1 TITL 2 15N RESONANCE ASSIGNMENTS OF THE HUMAN PTK6 SH2 DOMAIN
REMARK 1 REF J.BIOMOL.NMR V. 19 291 2001
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1011221125013
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RJA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-NOV-03.
REMARK 100 THE RCSB ID CODE IS RCSB020796.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.15
REMARK 210 PRESSURE : 1ATM
REMARK 210 SAMPLE CONTENTS : 1MM SH2 DOMAIN U-15N; 50MM
REMARK 210 PHOSPAHTE BUFFER NA; 90% H2O, 10%
REMARK 210 D2O; 1MM SH2 DOMAIN U-15N, 13C;
REMARK 210 50MM PHOSPAHTE BUFFER NA; 90%
REMARK 210 H2O, 10% D2O; 1MM SH2 DOMAIN U-
REMARK 210 15N, 13C; 50MM PHOSPAHTE BUFFER
REMARK 210 NA; 100% D2O; 1MM SH2 DOMAIN U-
REMARK 210 13C; 50MM PHOSPAHTE BUFFER NA;
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE 1.8, SPARKY
REMARK 210 3.106, INSIGHTII 98
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
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 H PHE A 6 O ILE A 30 1.58
REMARK 500 OD1 ASN A 23 H ARG A 97 1.58
REMARK 500 H VAL A 44 O ARG A 51 1.59
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 2 107.51 -178.54
REMARK 500 1 TRP A 4 86.27 85.34
REMARK 500 1 ALA A 20 169.27 -42.12
REMARK 500 1 ALA A 24 46.81 -92.45
REMARK 500 1 THR A 25 126.55 79.18
REMARK 500 1 ARG A 31 -168.68 -112.75
REMARK 500 1 PRO A 36 -156.24 -59.35
REMARK 500 1 ALA A 38 62.92 36.85
REMARK 500 1 ASP A 46 -90.27 55.46
REMARK 500 1 THR A 47 17.44 -149.25
REMARK 500 1 GLN A 48 -90.19 175.83
REMARK 500 1 ALA A 49 -168.64 -62.05
REMARK 500 1 ARG A 58 30.91 -91.25
REMARK 500 1 ALA A 59 77.36 41.03
REMARK 500 1 ARG A 62 113.53 -171.14
REMARK 500 1 LEU A 86 -89.68 -40.22
REMARK 500 1 LEU A 90 115.59 -166.63
REMARK 500 1 LEU A 92 170.71 -46.02
REMARK 500 1 ALA A 93 -84.88 -152.38
REMARK 500 1 LYS A 98 -153.99 -132.88
REMARK 500 2 GLU A 2 75.02 -178.78
REMARK 500 2 TRP A 4 90.92 75.76
REMARK 500 2 ALA A 20 173.86 -48.19
REMARK 500 2 THR A 25 141.97 56.63
REMARK 500 2 SER A 33 101.81 -53.00
REMARK 500 2 PRO A 36 -162.99 -57.73
REMARK 500 2 ASP A 46 -95.81 53.55
REMARK 500 2 GLN A 48 -73.80 -161.81
REMARK 500 2 ALA A 49 -173.10 -66.52
REMARK 500 2 ARG A 62 110.17 173.88
REMARK 500 2 GLU A 67 21.72 -79.75
REMARK 500 2 ALA A 68 13.46 -148.02
REMARK 500 2 LEU A 72 -39.21 -24.16
REMARK 500 2 LEU A 92 96.78 -46.73
REMARK 500 2 ALA A 93 -79.64 -90.28
REMARK 500 2 LYS A 98 -83.30 -138.81
REMARK 500 3 TRP A 4 93.97 76.23
REMARK 500 3 ALA A 20 172.09 -45.98
REMARK 500 3 ALA A 24 61.07 -108.63
REMARK 500 3 THR A 25 137.93 60.94
REMARK 500 3 SER A 33 91.05 -51.87
REMARK 500 3 PRO A 36 -176.80 -54.95
REMARK 500 3 SER A 37 -93.06 -84.17
REMARK 500 3 ALA A 38 61.83 -114.16
REMARK 500 3 ASP A 39 -161.62 -126.76
REMARK 500 3 ASP A 46 26.86 42.89
REMARK 500 3 THR A 47 -27.25 102.10
REMARK 500 3 GLN A 48 -114.01 -158.79
REMARK 500 3 ARG A 58 37.59 -92.01
REMARK 500 3 ALA A 59 73.07 45.49
REMARK 500
REMARK 500 THIS ENTRY HAS 429 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4902 RELATED DB: BMRB
DBREF 1RJA A 1 100 UNP Q13882 PTK6_HUMAN 75 174
SEQRES 1 A 100 SER GLU PRO TRP PHE PHE GLY CYS ILE SER ARG SER GLU
SEQRES 2 A 100 ALA VAL ARG ARG LEU GLN ALA GLU GLY ASN ALA THR GLY
SEQRES 3 A 100 ALA PHE LEU ILE ARG VAL SER GLU LYS PRO SER ALA ASP
SEQRES 4 A 100 TYR VAL LEU SER VAL ARG ASP THR GLN ALA VAL ARG HIS
SEQRES 5 A 100 TYR LYS ILE TRP ARG ARG ALA GLY GLY ARG LEU HIS LEU
SEQRES 6 A 100 ASN GLU ALA VAL SER PHE LEU SER LEU PRO GLU LEU VAL
SEQRES 7 A 100 ASN TYR HIS ARG ALA GLN SER LEU SER HIS GLY LEU ARG
SEQRES 8 A 100 LEU ALA ALA PRO CYS ARG LYS HIS GLU
HELIX 1 1 SER A 10 GLN A 19 1 10
HELIX 2 2 SER A 73 GLN A 84 1 12
SHEET 1 A 5 PHE A 28 VAL A 32 0
SHEET 2 A 5 TYR A 40 VAL A 44 -1 O VAL A 41 N ARG A 31
SHEET 3 A 5 ARG A 51 ARG A 57 -1 O ARG A 51 N VAL A 44
SHEET 4 A 5 LEU A 63 ASN A 66 -1 O HIS A 64 N TRP A 56
SHEET 5 A 5 VAL A 69 PHE A 71 -1 O PHE A 71 N LEU A 63
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