Header list of 1yiu.pdb file
Complete list - 2 20 Bytes
HEADER LIGASE 13-JAN-05 1YIU
TITLE ITCH E3 UBIQUITIN LIGASE WW3 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ITCHY E3 UBIQUITIN PROTEIN LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: WW3;
COMPND 5 EC: 6.3.2.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ITCH E3 WW3 DOMAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24D
KEYWDS WW DOMAIN, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 8
AUTHOR A.Z.SHAW,P.MARTIN-MALPARTIDA,B.MORALES,F.YRAOLA,M.ROYO,M.J.MACIAS
REVDAT 3 02-MAR-22 1YIU 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1YIU 1 VERSN
REVDAT 1 02-AUG-05 1YIU 0
JRNL AUTH A.Z.SHAW,P.MARTIN-MALPARTIDA,B.MORALES,F.YRAOLA,M.ROYO,
JRNL AUTH 2 M.J.MACIAS
JRNL TITL PHOSPHORYLATION OF EITHER SER16 OR THR30 DOES NOT DISRUPT
JRNL TITL 2 THE STRUCTURE OF THE ITCH E3 UBIQUITIN LIGASE THIRD WW
JRNL TITL 3 DOMAIN
JRNL REF PROTEINS V. 60 558 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 15971201
JRNL DOI 10.1002/PROT.20466
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3, ARIA 2.0A, CNS 1.1
REMARK 3 AUTHORS : BRUKER GMBH (XWINNMR), NILGES, M. (ARIA), BRUENGER
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE EMPLOYED REFINEMENT ENGINE WAS CNS
REMARK 3 1.1 , BUT USING THE WATER REFINEMENT CNS SCRIPTS SUPPLIED WITH
REMARK 3 ARIA 2.0A
REMARK 4
REMARK 4 1YIU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031562.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NA2HPO4 20MM NACL 100MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : UNLABELED SAMPLE; UNIFORM
REMARK 210 LABELING WITH 15N; UNIFORM
REMARK 210 LABELING WITH 15N, 13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.2, XEASY 1.3, CNS 1.1,
REMARK 210 ARIA 2.0A
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 OD1 ASP A 15 H ARG A 19 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 ALA A 2 70.05 57.45
REMARK 500 1 PRO A 8 97.07 -40.91
REMARK 500 1 ARG A 36 42.68 -91.81
REMARK 500 2 PRO A 5 -157.09 -69.18
REMARK 500 2 PRO A 8 98.28 -39.68
REMARK 500 3 MET A 3 -84.60 67.04
REMARK 500 3 PRO A 8 106.54 -49.45
REMARK 500 3 ARG A 36 48.29 -81.97
REMARK 500 4 PRO A 5 150.70 -45.75
REMARK 500 4 PRO A 8 98.64 -42.66
REMARK 500 4 ARG A 28 67.88 63.42
REMARK 500 5 PRO A 8 100.61 -54.78
REMARK 500 6 PRO A 8 100.83 -50.14
REMARK 500 6 ARG A 28 63.42 60.96
REMARK 500 7 PRO A 8 98.23 -34.40
REMARK 500 7 ARG A 28 61.14 60.38
REMARK 500 7 ARG A 36 -73.18 -68.09
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YIU A 4 37 UNP Q8C863 ITCH_MOUSE 399 432
SEQADV 1YIU GLY A 1 UNP Q8C863 CLONING ARTIFACT
SEQADV 1YIU ALA A 2 UNP Q8C863 CLONING ARTIFACT
SEQADV 1YIU MET A 3 UNP Q8C863 CLONING ARTIFACT
SEQRES 1 A 37 GLY ALA MET GLY PRO LEU PRO PRO GLY TRP GLU LYS ARG
SEQRES 2 A 37 THR ASP SER ASN GLY ARG VAL TYR PHE VAL ASN HIS ASN
SEQRES 3 A 37 THR ARG ILE THR GLN TRP GLU ASP PRO ARG SER
SHEET 1 A 3 LYS A 12 THR A 14 0
SHEET 2 A 3 VAL A 20 ASN A 24 -1 O TYR A 21 N ARG A 13
SHEET 3 A 3 ILE A 29 GLN A 31 -1 O GLN A 31 N PHE A 22
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 - 2 20 Bytes