Header list of 1awx.pdb file
Complete list - 16 20 Bytes
HEADER TRANSFERASE 06-OCT-97 1AWX
TITLE SH3 DOMAIN FROM BRUTON'S TYROSINE KINASE, NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRUTON'S TYROSINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: ATK, AGMX1, BPK;
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 TISSUE: BLOOD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-3
KEYWDS TYROSINE KINASE, X-LINKED AGAMMAGLOBULINEMIA, XLA, BTK, SH3 DOMAIN,
KEYWDS 2 TRANSFERASE
EXPDTA SOLUTION NMR
AUTHOR H.HANSSON,P.T.MATTSSON,P.ALLARD,P.HAAPANIEMI,M.VIHINEN,C.I.E.SMITH,
AUTHOR 2 T.HARD
REVDAT 4 16-FEB-22 1AWX 1 REMARK
REVDAT 3 24-FEB-09 1AWX 1 VERSN
REVDAT 2 01-APR-03 1AWX 1 JRNL
REVDAT 1 08-APR-98 1AWX 0
JRNL AUTH H.HANSSON,P.T.MATTSSON,P.ALLARD,P.HAAPANIEMI,M.VIHINEN,
JRNL AUTH 2 C.I.SMITH,T.HARD
JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN FROM BRUTON'S TYROSINE
JRNL TITL 2 KINASE.
JRNL REF BIOCHEMISTRY V. 37 2912 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9485443
JRNL DOI 10.1021/BI972409F
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: THE STRUCTURE WAS DETERMINED USING 756
REMARK 3 DISTANCE RESTRAINTS, 52 DIHEDRAL ANGLE RESTRAINTS AND 22
REMARK 3 HYDROGEN BOND RESTRAINTS. THE HYDROGEN BOND RESTRAINTS WERE USED
REMARK 3 ONLY IN THE LAST STEP OF REFINEMENT. 50 STRUCTURES WERE
REMARK 3 CALCULATED AND REFINED USING AB INITIO SIMULATED ANNEALING
REMARK 3 PROTOCOL FOR X-PLOR (1). ALL FORCE CONSTANTS AND POTENTIALS WERE
REMARK 3 SET TO THE DEFAULT (PROTOCOL) VALUES EXCEPT FOR THE VAN DER
REMARK 3 WAALS' RADII SCALE FACTOR ("REPEL"), WHICH WAS DECREASED TO 0.80
REMARK 3 INSTEAD OF 0.75 DURING THE FINAL COOLING STAGES IN THE
REMARK 3 REFINEMENT. THIS RESULTS IN MORE REASONABLE BACKBONE
REMARK 3 CONFORMATION AND SOMEWHAT HIGHER X-PLOR TOTAL ENERGIES. CENTER
REMARK 3 AVERAGING PSEUDOATOM CORRECTION WAS USED FOR ALL DISTANCE
REMARK 3 RESTRAINT S(2). ON THE BASIS OF X-PLOR TOTAL ENERGY 42 LOWEST
REMARK 3 ENERGY STRUCTURES WERE SELECTED. THE AVERAGE AND MINIMIZED
REMARK 3 STRUCTURE WAS CALCULATED BY AVERAGING SUPERIMPOSED STRUCTURES IN
REMARK 3 THE ENSEMBLE AND THEN ENERGY MINIMIZING THE AVERAGE STRUCTURE.
REMARK 3 THE POTENTIALS AND CONSTANTS USED IN THE ENERGY MINIMIZATION
REMARK 3 WERE THE SAME FOR THE AVERAGE STRUCTURE AND THE ENSEMBLE
REMARK 3 STRUCTURES.
REMARK 4
REMARK 4 1AWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171356.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; 15N
REMARK 210 -TOCSY-HSQC; 15N-NOESY-HSQC;
REMARK 210 HNHA; HNHB
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 : VNMR 4.3 AND 5.2, ANSIG V.3.2
REMARK 210 V.3.2, X-PLOR V.3.851 V.3.851
REMARK 210 METHOD USED : AB INITIO - SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE
REMARK 210 BASED ON 42 LOWEST ENERGY
REMARK 210 STRUCTURES
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: 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 MET A 3 91.10 52.82
REMARK 500 SER A 6 -72.51 -59.56
REMARK 500 LEU A 8 115.68 -161.33
REMARK 500 LEU A 14 -70.95 -91.67
REMARK 500 TYR A 17 93.15 -167.56
REMARK 500 ASN A 21 -55.19 -125.35
REMARK 500 ALA A 22 -40.23 -170.66
REMARK 500 LEU A 27 -168.97 -79.77
REMARK 500 ARG A 28 -158.33 -169.99
REMARK 500 GLU A 37 -162.28 -123.81
REMARK 500 GLU A 38 43.49 177.99
REMARK 500 SER A 39 -171.18 -54.13
REMARK 500 TRP A 44 -161.66 -110.22
REMARK 500 ASP A 48 -152.70 -98.80
REMARK 500 LYS A 49 36.48 -95.93
REMARK 500 THR A 62 -133.42 -145.06
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 ARG A 28 0.30 SIDE CHAIN
REMARK 500 ARG A 45 0.28 SIDE CHAIN
REMARK 500 ARG A 47 0.22 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AWW RELATED DB: PDB
DBREF 1AWX A 4 67 UNP Q06187 BTK_HUMAN 212 275
SEQRES 1 A 67 GLY SER MET SER THR SER GLU LEU LYS LYS VAL VAL ALA
SEQRES 2 A 67 LEU TYR ASP TYR MET PRO MET ASN ALA ASN ASP LEU GLN
SEQRES 3 A 67 LEU ARG LYS GLY ASP GLU TYR PHE ILE LEU GLU GLU SER
SEQRES 4 A 67 ASN LEU PRO TRP TRP ARG ALA ARG ASP LYS ASN GLY GLN
SEQRES 5 A 67 GLU GLY TYR ILE PRO SER ASN TYR VAL THR GLU ALA GLU
SEQRES 6 A 67 ASP SER
SHEET 1 A 2 LYS A 10 VAL A 12 0
SHEET 2 A 2 GLU A 32 PHE A 34 -1 N TYR A 33 O VAL A 11
SHEET 1 B 2 TRP A 43 ARG A 47 0
SHEET 2 B 2 GLU A 53 PRO A 57 -1 N ILE A 56 O TRP A 44
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
Complete list - 16 20 Bytes