Header list of 1ttn.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 23-JUN-04 1TTN
TITLE SOLUTION STRUCTURE OF THE UBIQUITIN-LIKE DOMAIN OF HUMAN DC-UBP FROM
TITLE 2 DENDRITIC CELLS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DENDRITIC CELL-DERIVED UBIQUITIN-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBIQUITIN-LIKE DOMAIN;
COMPND 5 SYNONYM: DC-UBP;
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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)
KEYWDS UBIQUITIN-LIKE DOMAIN, DC-UBP, SOLUTION STRUCTURE, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
MDLTYP MINIMIZED AVERAGE
AUTHOR H.Y.HU
REVDAT 4 02-MAR-22 1TTN 1 REMARK
REVDAT 3 24-FEB-09 1TTN 1 VERSN
REVDAT 2 16-AUG-05 1TTN 1 JRNL
REVDAT 1 05-JUL-05 1TTN 0
JRNL AUTH Y.G.GAO,A.X.SONG,Y.H.SHI,Y.G.CHANG,S.X.LIU,Y.Z.YU,X.T.CAO,
JRNL AUTH 2 D.H.LIN,H.Y.HU
JRNL TITL SOLUTION STRUCTURE OF THE UBIQUITIN-LIKE DOMAIN OF HUMAN
JRNL TITL 2 DC-UBP FROM DENDRITIC CELLS
JRNL REF PROTEIN SCI. V. 14 2044 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 15987890
JRNL DOI 10.1110/PS.051455505
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS 1.1, ARIA 1.2
REMARK 3 AUTHORS : VARIAN (XWINNMR), A.T.BRUNGER ET AL. (CNS), JENS
REMARK 3 LINGE ET AL. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 901 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS,83 DIHEDRAL ANGLE RESTRAINTS,60
REMARK 3 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1TTN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022892.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1.2MM UBIQUITIN-LIKE DOMAIN OF
REMARK 210 DC-UBP ,10MM NAAC, 100MM NACL,
REMARK 210 5MM DTT, 0.02% SODIUM AZIDE;
REMARK 210 1.2MM UBIQUITIN-LIKE DOMAIN OF
REMARK 210 DC-UBP ,10MM NAAC, 100MM NACL,
REMARK 210 5MM DTT, 0.02% SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 1-15
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 LYS A 5
REMARK 465 SER A 6
REMARK 465 ASP A 7
REMARK 465 ILE A 8
REMARK 465 GLU A 9
REMARK 465 THR A 10
REMARK 465 LEU A 11
REMARK 465 ASP A 12
REMARK 465 ILE A 13
REMARK 465 PRO A 14
REMARK 465 GLU A 15
REMARK 465 PRO A 16
REMARK 465 PRO A 17
REMARK 465 PRO A 18
REMARK 465 ASN A 19
REMARK 465 SER A 20
REMARK 465 PRO A 101
REMARK 465 THR A 102
REMARK 465 PRO A 103
REMARK 465 VAL A 104
REMARK 465 GLU A 105
REMARK 465 ASN A 106
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 O ARG A 41 H THR A 43 1.39
REMARK 500 O LEU A 30 H GLY A 33 1.54
REMARK 500 O ARG A 41 N THR A 43 2.04
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 TYR A 22 -61.43 -101.30
REMARK 500 1 SER A 31 7.97 48.36
REMARK 500 1 THR A 32 15.67 81.72
REMARK 500 1 LYS A 34 79.89 -117.93
REMARK 500 1 SER A 42 -47.95 29.05
REMARK 500 1 ASP A 44 -75.07 -80.35
REMARK 500 1 THR A 45 157.77 57.81
REMARK 500 1 VAL A 46 -31.95 -29.26
REMARK 500 1 PHE A 47 -70.04 -65.73
REMARK 500 1 PRO A 61 -152.45 -68.54
REMARK 500 1 GLN A 64 69.66 -107.26
REMARK 500 1 LYS A 76 31.70 -147.58
REMARK 500 1 GLU A 81 -65.60 -91.97
REMARK 500 1 LEU A 82 -7.01 70.05
REMARK 500 1 ILE A 84 61.98 -110.02
REMARK 500 1 LYS A 86 -36.40 178.33
REMARK 500 1 VAL A 98 25.66 -148.90
REMARK 500 1 GLN A 99 155.76 60.78
REMARK 500 2 TYR A 22 40.75 -96.15
REMARK 500 2 SER A 42 -47.80 42.75
REMARK 500 2 THR A 45 170.77 -48.12
REMARK 500 2 VAL A 46 -28.18 -34.31
REMARK 500 2 LYS A 78 -70.77 -57.16
REMARK 500 2 GLU A 81 -63.76 -92.12
REMARK 500 2 LEU A 82 -3.37 70.18
REMARK 500 2 LYS A 86 16.15 -158.95
REMARK 500 3 SER A 31 -55.68 57.24
REMARK 500 3 THR A 32 28.97 170.80
REMARK 500 3 SER A 42 -48.18 30.74
REMARK 500 3 ASP A 44 -77.15 -88.34
REMARK 500 3 THR A 45 156.11 59.19
REMARK 500 3 VAL A 46 -33.04 -27.93
REMARK 500 3 LYS A 78 -70.37 -57.24
REMARK 500 3 LEU A 82 -36.20 78.77
REMARK 500 3 PRO A 85 49.46 -85.87
REMARK 500 3 LYS A 86 -79.83 -151.51
REMARK 500 3 VAL A 98 -47.22 -139.82
REMARK 500 4 TYR A 22 -47.23 -147.45
REMARK 500 4 GLU A 23 -67.89 -102.87
REMARK 500 4 SER A 42 -48.16 34.44
REMARK 500 4 ASP A 44 -77.85 -75.82
REMARK 500 4 THR A 45 156.89 59.00
REMARK 500 4 VAL A 46 -34.31 -27.01
REMARK 500 4 PHE A 47 -70.01 -62.79
REMARK 500 4 PRO A 61 -153.86 -59.37
REMARK 500 4 LYS A 76 37.21 -156.09
REMARK 500 4 LEU A 82 -14.10 74.15
REMARK 500 4 PRO A 85 60.54 -69.94
REMARK 500 4 LYS A 86 -89.37 -166.80
REMARK 500 4 SER A 95 52.88 -146.19
REMARK 500
REMARK 500 THIS ENTRY HAS 194 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TTN A 1 106 UNP Q8WUN7 Q8WUN7_HUMAN 85 190
SEQRES 1 A 106 MET ILE GLU GLU LYS SER ASP ILE GLU THR LEU ASP ILE
SEQRES 2 A 106 PRO GLU PRO PRO PRO ASN SER GLY TYR GLU CYS GLN LEU
SEQRES 3 A 106 ARG LEU ARG LEU SER THR GLY LYS ASP LEU LYS LEU VAL
SEQRES 4 A 106 VAL ARG SER THR ASP THR VAL PHE HIS MET LYS ARG ARG
SEQRES 5 A 106 LEU HIS ALA ALA GLU GLY VAL GLU PRO GLY SER GLN ARG
SEQRES 6 A 106 TRP PHE PHE SER GLY ARG PRO LEU THR ASP LYS MET LYS
SEQRES 7 A 106 PHE GLU GLU LEU LYS ILE PRO LYS ASP TYR VAL VAL GLN
SEQRES 8 A 106 VAL ILE VAL SER GLN PRO VAL GLN ASN PRO THR PRO VAL
SEQRES 9 A 106 GLU ASN
HELIX 1 1 ASP A 44 ALA A 56 1 13
HELIX 2 2 MET A 77 LEU A 82 1 6
SHEET 1 A 5 LYS A 34 VAL A 40 0
SHEET 2 A 5 CYS A 24 LEU A 30 -1 N CYS A 24 O VAL A 40
SHEET 3 A 5 VAL A 89 ILE A 93 1 O VAL A 90 N ARG A 29
SHEET 4 A 5 ARG A 65 PHE A 68 -1 N PHE A 67 O GLN A 91
SHEET 5 A 5 ARG A 71 PRO A 72 -1 O ARG A 71 N PHE A 68
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