Header list of 2cwb.pdb file
Complete list - 15 20 Bytes
HEADER PROTEIN BINDING 17-JUN-05 2CWB
TITLE SOLUTION STRUCTURE OF THE UBIQUITIN-ASSOCIATED DOMAIN OF HUMAN BMSC-
TITLE 2 UBP AND ITS COMPLEX WITH UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN G-BINDING PROTEIN G,UBIQUITIN-LIKE PROTEIN
COMPND 3 7;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: C-TERMINAL UBA DOMAIN,C-TERMINAL UBA DOMAIN;
COMPND 6 SYNONYM: IGG-BINDING PROTEIN G,BONE MARROW STROMAL CELL UBIQUITIN-
COMPND 7 LIKE PROTEIN,BMSC-UBP,UBIQUITIN-LIKE PROTEIN SB132;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: A SOLUBILITY-ENHANCEMENT TAG (SET) GB1, IMMUNOGLOBULIN
COMPND 11 G BINDING DOMAIN 1 OF STREPTOCOCCAL PROTEIN G, WAS USED TO ENHANCE
COMPND 12 THE SOLUBILITY OF THE UBA DOMAIN OF BMSC-UBP. THE SEQUENCE OF THE
COMPND 13 CHIMERICAL HGB1-UBA IS AS
COMPND 14 FOLLOWS:MHHHHHHQYKLALNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVT
COMPND 15 EGSQWQPQLQQLRDMGIQDDELSLRALQATGGDIQAALELIFAGGAP.,A SOLUBILITY-
COMPND 16 ENHANCEMENT TAG (SET) GB1, IMMUNOGLOBULIN G BINDING DOMAIN 1 OF
COMPND 17 STREPTOCOCCAL PROTEIN G, WAS USED TO ENHANCE THE SOLUBILITY OF THE
COMPND 18 UBA DOMAIN OF BMSC-UBP. THE SEQUENCE OF THE CHIMERICAL HGB1-UBA IS AS
COMPND 19 FOLLOWS:MHHHHHHQYKLALNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVT
COMPND 20 EGSQWQPQLQQLRDMGIQDDELSLRALQATGGDIQAALELIFAGGAP.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP. GROUP G, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 1320, 9606;
SOURCE 5 GENE: SPG, UBL7, BMSCUBP, SB132;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHGB
KEYWDS HELICAL BUNDLE, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Y.G.CHANG,A.X.SONG,Y.G.GAO,Y.H.SHI,X.J.LIN,X.T.CAO,D.H.LIN,H.Y.HU
REVDAT 4 15-JAN-20 2CWB 1 COMPND SOURCE REMARK DBREF
REVDAT 4 2 1 SEQADV
REVDAT 3 24-FEB-09 2CWB 1 VERSN
REVDAT 2 13-JUN-06 2CWB 1 JRNL
REVDAT 1 06-JUN-06 2CWB 0
JRNL AUTH Y.G.CHANG,A.X.SONG,Y.G.GAO,Y.H.SHI,X.J.LIN,X.T.CAO,D.H.LIN,
JRNL AUTH 2 H.Y.HU
JRNL TITL SOLUTION STRUCTURE OF THE UBIQUITIN-ASSOCIATED DOMAIN OF
JRNL TITL 2 HUMAN BMSC-UBP AND ITS COMPLEX WITH UBIQUITIN.
JRNL REF PROTEIN SCI. V. 15 1248 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16731964
JRNL DOI 10.1110/PS.051995006
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, ARIA 1.2
REMARK 3 AUTHORS : F.DELAGLIO, S.GRZESIEK, G.W.VUISTER, G.ZHU,
REMARK 3 J.PFEIFER, A.BAX (NMRPIPE), J.LINGE, S.O.DONOGHUE,
REMARK 3 M.NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CWB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024697.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HGB1-UBA U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
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 : SPARKY, ARIA 1.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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.
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 GLN A 8
REMARK 465 TYR A 9
REMARK 465 LYS A 10
REMARK 465 LEU A 11
REMARK 465 ALA A 12
REMARK 465 LEU A 13
REMARK 465 ASN A 14
REMARK 465 GLY A 15
REMARK 465 LYS A 16
REMARK 465 THR A 17
REMARK 465 LEU A 18
REMARK 465 LYS A 19
REMARK 465 GLY A 20
REMARK 465 GLU A 21
REMARK 465 THR A 22
REMARK 465 THR A 23
REMARK 465 THR A 24
REMARK 465 GLU A 25
REMARK 465 ALA A 26
REMARK 465 VAL A 27
REMARK 465 ASP A 28
REMARK 465 ALA A 29
REMARK 465 ALA A 30
REMARK 465 THR A 31
REMARK 465 ALA A 32
REMARK 465 GLU A 33
REMARK 465 LYS A 34
REMARK 465 VAL A 35
REMARK 465 PHE A 36
REMARK 465 LYS A 37
REMARK 465 GLN A 38
REMARK 465 TYR A 39
REMARK 465 ALA A 40
REMARK 465 ASN A 41
REMARK 465 ASP A 42
REMARK 465 ASN A 43
REMARK 465 GLY A 44
REMARK 465 VAL A 45
REMARK 465 ASP A 46
REMARK 465 GLY A 47
REMARK 465 GLU A 48
REMARK 465 TRP A 49
REMARK 465 THR A 50
REMARK 465 TYR A 51
REMARK 465 ASP A 52
REMARK 465 ASP A 53
REMARK 465 ALA A 54
REMARK 465 THR A 55
REMARK 465 LYS A 56
REMARK 465 THR A 57
REMARK 465 PHE A 58
REMARK 465 THR A 59
REMARK 465 VAL A 60
REMARK 465 THR A 61
REMARK 465 GLU A 62
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 GLN A 65 -10.69 71.50
REMARK 500 1 ALA A 107 149.22 -172.95
REMARK 500 4 ALA A 104 39.47 -157.65
REMARK 500 6 ALA A 107 70.85 59.46
REMARK 500 7 ASP A 80 47.79 -84.94
REMARK 500 7 ALA A 104 -27.89 -148.19
REMARK 500 8 SER A 64 -163.72 -173.32
REMARK 500 10 ALA A 107 88.62 172.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2CWB A 9 62 UNP P06654 SPG1_STRSG 229 282
DBREF 2CWB A 64 108 UNP Q96S82 UBL7_HUMAN 336 380
SEQADV 2CWB MET A 1 UNP P06654 EXPRESSION TAG
SEQADV 2CWB HIS A 2 UNP P06654 EXPRESSION TAG
SEQADV 2CWB HIS A 3 UNP P06654 EXPRESSION TAG
SEQADV 2CWB HIS A 4 UNP P06654 EXPRESSION TAG
SEQADV 2CWB HIS A 5 UNP P06654 EXPRESSION TAG
SEQADV 2CWB HIS A 6 UNP P06654 EXPRESSION TAG
SEQADV 2CWB HIS A 7 UNP P06654 EXPRESSION TAG
SEQADV 2CWB GLN A 8 UNP P06654 EXPRESSION TAG
SEQADV 2CWB ALA A 12 UNP P06654 ILE 232 ENGINEERED MUTATION
SEQADV 2CWB GLY A 63 UNP P06654 LINKER
SEQRES 1 A 108 MET HIS HIS HIS HIS HIS HIS GLN TYR LYS LEU ALA LEU
SEQRES 2 A 108 ASN GLY LYS THR LEU LYS GLY GLU THR THR THR GLU ALA
SEQRES 3 A 108 VAL ASP ALA ALA THR ALA GLU LYS VAL PHE LYS GLN TYR
SEQRES 4 A 108 ALA ASN ASP ASN GLY VAL ASP GLY GLU TRP THR TYR ASP
SEQRES 5 A 108 ASP ALA THR LYS THR PHE THR VAL THR GLU GLY SER GLN
SEQRES 6 A 108 TRP GLN PRO GLN LEU GLN GLN LEU ARG ASP MET GLY ILE
SEQRES 7 A 108 GLN ASP ASP GLU LEU SER LEU ARG ALA LEU GLN ALA THR
SEQRES 8 A 108 GLY GLY ASP ILE GLN ALA ALA LEU GLU LEU ILE PHE ALA
SEQRES 9 A 108 GLY GLY ALA PRO
HELIX 1 1 TRP A 66 ASP A 75 1 10
HELIX 2 2 ASP A 80 GLY A 92 1 13
HELIX 3 3 ASP A 94 GLY A 105 1 12
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 - 15 20 Bytes