Header list of 1zbj.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 08-APR-05 1ZBJ
TITLE INFERENTIAL STRUCTURE DETERMINATION OF THE FYN SH3 DOMAIN USING NOESY
TITLE 2 DATA FROM A 15N,H2 ENRICHED PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FYN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 83-141;
COMPND 5 SYNONYM: P59-FYN, SYN, SLK;
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 GENE: FYN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.RIEPING,M.HABECK,M.NILGES
REVDAT 4 02-MAR-22 1ZBJ 1 REMARK
REVDAT 3 24-FEB-09 1ZBJ 1 VERSN
REVDAT 2 02-AUG-05 1ZBJ 1 JRNL
REVDAT 1 03-MAY-05 1ZBJ 0
JRNL AUTH W.RIEPING,M.HABECK,M.NILGES
JRNL TITL INFERENTIAL STRUCTURE DETERMINATION
JRNL REF SCIENCE V. 309 303 2005
JRNL REFN ISSN 0036-8075
JRNL PMID 16002620
JRNL DOI 10.1126/SCIENCE.1110428
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.K.MAL,S.J.MATTHEWS,H.KOVACS,I.D.CAMPBELL,J.BOYD
REMARK 1 TITL SOME NMR EXPERIMENTS AND A STRUCTURE DETERMINATION EMPLOYING
REMARK 1 TITL 2 A [15N,2H] ENRICHED PROTEIN
REMARK 1 REF J.BIOMOL.NMR V. 12 259 1998
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 9751998
REMARK 1 DOI 10.1023/A:1008238009056
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ISD 1.0
REMARK 3 AUTHORS : HABECK, RIEPING
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZBJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032532.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : INFERENTIAL STRUCTURE
REMARK 210 DETERMINATION, MARKOV CHAIN
REMARK 210 MONTE CARLO SAMPLING, REPLICA-
REMARK 210 EXCHANGE MONTE CARLO, GIBBS
REMARK 210 SAMPLING, HYBRID MONTE CARLO,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : HIGH POSTERIOR PROBABILITY
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: 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 LEU A 7 -63.62 -98.30
REMARK 500 1 ARG A 13 50.08 -115.52
REMARK 500 1 LEU A 29 -45.78 -163.03
REMARK 500 1 SER A 31 65.23 -155.47
REMARK 500 1 SER A 32 -67.25 -91.42
REMARK 500 1 GLU A 33 -62.11 -161.79
REMARK 500 1 ASP A 35 -100.58 -151.07
REMARK 500 1 THR A 43 -79.82 -114.06
REMARK 500 1 SER A 52 49.37 -96.97
REMARK 500 1 PRO A 57 -169.30 -79.92
REMARK 500 2 ASP A 16 -68.84 -128.77
REMARK 500 2 LEU A 29 -75.82 -143.82
REMARK 500 2 SER A 31 67.37 -152.49
REMARK 500 2 SER A 32 -92.27 -82.29
REMARK 500 2 GLU A 33 -81.56 -105.66
REMARK 500 2 ASP A 35 -78.90 -147.31
REMARK 500 2 THR A 43 -92.82 -83.30
REMARK 500 2 TYR A 54 36.29 -155.40
REMARK 500 2 VAL A 58 -169.89 -117.99
REMARK 500 3 THR A 2 -63.50 -104.58
REMARK 500 3 LEU A 7 -60.71 -134.58
REMARK 500 3 ARG A 13 68.03 -168.22
REMARK 500 3 PHE A 20 -164.04 -129.78
REMARK 500 3 LEU A 29 -93.63 -155.98
REMARK 500 3 SER A 32 68.15 -156.89
REMARK 500 3 GLU A 33 -77.23 -140.19
REMARK 500 3 ARG A 40 -163.88 -110.88
REMARK 500 3 THR A 43 -60.43 -106.60
REMARK 500 3 THR A 44 -60.83 -93.06
REMARK 500 4 THR A 2 -96.20 -84.64
REMARK 500 4 TYR A 10 85.02 -155.75
REMARK 500 4 ALA A 12 -154.32 -143.87
REMARK 500 4 ARG A 13 59.70 -175.07
REMARK 500 4 ASP A 16 -72.62 -93.62
REMARK 500 4 ASP A 17 99.07 -67.50
REMARK 500 4 LEU A 18 -158.19 -89.21
REMARK 500 4 LEU A 29 -69.00 -158.07
REMARK 500 4 SER A 31 63.72 -167.57
REMARK 500 4 GLU A 33 69.55 65.51
REMARK 500 4 ASP A 35 -73.36 -129.74
REMARK 500 4 THR A 43 -71.14 -94.94
REMARK 500 4 VAL A 58 -169.15 -111.92
REMARK 500 5 ARG A 13 46.79 -155.44
REMARK 500 5 LEU A 29 -73.54 -154.42
REMARK 500 5 SER A 31 86.95 -162.56
REMARK 500 5 SER A 32 -108.42 -92.05
REMARK 500 5 GLU A 33 -78.01 -83.83
REMARK 500 5 ASP A 35 -89.70 -145.59
REMARK 500 5 THR A 47 -165.35 -114.51
REMARK 500 5 SER A 52 58.78 -117.09
REMARK 500
REMARK 500 THIS ENTRY HAS 183 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NYF RELATED DB: PDB
REMARK 900 NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE
REMARK 900 RELATED ID: 1SHF RELATED DB: PDB
REMARK 900 FYN PROTO-ONCOGENE TYROSINE KINASE (SH3 DOMAIN)
DBREF 1ZBJ A 1 59 UNP P06241 FYN_HUMAN 83 141
SEQRES 1 A 59 VAL THR LEU PHE VAL ALA LEU TYR ASP TYR GLU ALA ARG
SEQRES 2 A 59 THR GLU ASP ASP LEU SER PHE HIS LYS GLY GLU LYS PHE
SEQRES 3 A 59 GLN ILE LEU ASN SER SER GLU GLY ASP TRP TRP GLU ALA
SEQRES 4 A 59 ARG SER LEU THR THR GLY GLU THR GLY TYR ILE PRO SER
SEQRES 5 A 59 ASN TYR VAL ALA PRO VAL ASP
SHEET 1 A 2 PHE A 4 VAL A 5 0
SHEET 2 A 2 LYS A 25 PHE A 26 -1 O PHE A 26 N PHE A 4
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 2 2 Bytes