Header list of 1w1f.pdb file
Complete list - n 15 2 Bytes
HEADER SH3-DOMAIN 21-JUN-04 1W1F
TITLE SH3 DOMAIN OF HUMAN LYN TYROSINE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE LYN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 60-122;
COMPND 5 EC: 2.7.1.112;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2
KEYWDS SH3-DOMAIN, SH3 DOMAIN, TYROSINE KINASE, SIGNAL TRANSDUCTION, LYN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.BAUER,K.SCHWEIMER,S.HOFFMANN,P.ROESCH,H.STICHT
REVDAT 4 15-JAN-20 1W1F 1 REMARK
REVDAT 3 24-FEB-09 1W1F 1 VERSN
REVDAT 2 05-OCT-05 1W1F 1 JRNL
REVDAT 1 06-JUL-05 1W1F 0
JRNL AUTH F.BAUER,K.SCHWEIMER,H.MEISELBACH,S.HOFFMANN,P.ROESCH,
JRNL AUTH 2 H.STICHT
JRNL TITL STRUCTURAL CHARACTERIZATION OF LYN-SH3 DOMAIN IN COMPLEX
JRNL TITL 2 WITH A HERPESVIRAL PROTEIN REVEALS AN EXTENDED RECOGNITION
JRNL TITL 3 MOTIF THAT ENHANCES BINDING AFFINITY.
JRNL REF PROTEIN SCI. V. 14 2487 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 16155203
JRNL DOI 10.1110/PS.051563605
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: AB INITIO SIMULATED ANNEALING
REMARK 4
REMARK 4 1W1F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1290020169.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 150
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D 13C-; 15N-EDITED NOESY; 3D
REMARK 210 15N-EDITED NOESY; 3D 13C-EDITED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : OTHER
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW
REMARK 210 METHOD USED : X-PLOR
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED LYNSH3
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 GLU A 8
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 TYR A 19 O PHE A 29 1.53
REMARK 500 H ALA A 15 O GLU A 33 1.54
REMARK 500 O VAL A 13 H MET A 35 1.56
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 LYS A 31 152.07 -42.21
REMARK 500 1 ALA A 64 -165.47 -160.66
REMARK 500 1 LEU A 66 -171.75 45.39
REMARK 500 1 ASN A 67 -87.99 172.12
REMARK 500 2 LYS A 31 151.82 -44.19
REMARK 500 2 GLU A 43 -47.15 160.93
REMARK 500 2 LYS A 53 24.63 48.25
REMARK 500 2 ASN A 61 -1.65 -140.48
REMARK 500 3 LYS A 31 152.01 -42.79
REMARK 500 3 ALA A 64 -166.03 -160.38
REMARK 500 4 LYS A 31 152.44 -43.01
REMARK 500 4 GLU A 43 -48.18 158.70
REMARK 500 4 LYS A 53 11.88 59.56
REMARK 500 4 LEU A 66 80.95 -67.02
REMARK 500 5 ASP A 11 153.47 175.75
REMARK 500 5 LYS A 31 152.16 -41.83
REMARK 500 5 GLU A 43 -45.35 160.01
REMARK 500 6 LYS A 31 152.70 -42.86
REMARK 500 6 GLU A 43 -42.40 161.19
REMARK 500 6 LEU A 66 85.29 41.46
REMARK 500 7 ASP A 11 137.08 163.84
REMARK 500 7 LYS A 31 151.83 -43.73
REMARK 500 7 GLU A 43 -43.42 161.08
REMARK 500 7 SER A 60 30.06 -91.77
REMARK 500 7 ASN A 67 -172.05 55.38
REMARK 500 8 LYS A 31 152.01 -44.43
REMARK 500 8 GLU A 43 -48.84 156.37
REMARK 500 8 LYS A 53 25.38 44.44
REMARK 500 9 LYS A 31 152.06 -42.16
REMARK 500 9 HIS A 41 -157.77 -75.86
REMARK 500 9 GLU A 43 -40.15 163.51
REMARK 500 10 ASP A 11 141.02 177.96
REMARK 500 10 LYS A 31 153.55 -41.25
REMARK 500 10 GLU A 43 -42.87 162.36
REMARK 500 10 LEU A 66 -166.00 46.66
REMARK 500 11 LYS A 31 152.23 -43.63
REMARK 500 12 LYS A 31 151.21 -43.11
REMARK 500 12 ASN A 61 -2.67 -140.70
REMARK 500 12 LEU A 66 -91.25 63.33
REMARK 500 12 ASN A 67 110.71 174.17
REMARK 500 13 LYS A 31 152.66 -43.65
REMARK 500 13 ASN A 67 41.68 -88.42
REMARK 500 14 LYS A 31 151.47 -42.60
REMARK 500 14 LYS A 53 25.20 42.43
REMARK 500 14 ASN A 61 -4.23 -140.27
REMARK 500 14 LEU A 66 -71.99 77.99
REMARK 500 14 ASN A 67 -39.40 -145.80
REMARK 500 15 LYS A 31 154.51 -38.87
REMARK 500 15 LYS A 53 25.43 49.72
REMARK 500 15 ASN A 61 -0.10 -140.65
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6261 RELATED DB: BMRB
DBREF 1W1F A 4 5 PDB 1W1F 1W1F 4 5
DBREF 1W1F A 6 68 UNP P07948 LYN_HUMAN 60 122
SEQRES 1 A 65 GLY SER PRO GLU GLU GLN GLY ASP ILE VAL VAL ALA LEU
SEQRES 2 A 65 TYR PRO TYR ASP GLY ILE HIS PRO ASP ASP LEU SER PHE
SEQRES 3 A 65 LYS LYS GLY GLU LYS MET LYS VAL LEU GLU GLU HIS GLY
SEQRES 4 A 65 GLU TRP TRP LYS ALA LYS SER LEU LEU THR LYS LYS GLU
SEQRES 5 A 65 GLY PHE ILE PRO SER ASN TYR VAL ALA LYS LEU ASN THR
SHEET 1 AA 5 GLU A 55 PRO A 59 0
SHEET 2 AA 5 TRP A 44 SER A 49 -1 O TRP A 45 N ILE A 58
SHEET 3 AA 5 LYS A 34 GLU A 40 -1 O LYS A 36 N LYS A 48
SHEET 4 AA 5 ASP A 11 ALA A 15 -1 O ASP A 11 N VAL A 37
SHEET 5 AA 5 VAL A 63 ALA A 64 -1 O ALA A 64 N VAL A 14
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 - n 15 2 Bytes