Header list of 1x1f.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 04-APR-05 1X1F
TITLE SOLUTION STRUCTURE OF THE PH DOMAIN OF HUMAN DOCKING PROTEIN BRDG1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIGNAL-TRANSDUCING ADAPTOR PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PH DOMAIN;
COMPND 5 SYNONYM: STAP-1, STEM CELL ADAPTOR PROTEIN 1, BCR DOWNSTREAM
COMPND 6 SIGNALING PROTEIN 1, DOCKING PROTEIN BRDG1;
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: BRDG1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040301-57;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS DOCKING PROTEIN BRDG1, PH DOMAIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING
KEYWDS 4 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X1F 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X1F 1 VERSN
REVDAT 1 04-OCT-05 1X1F 0
JRNL AUTH H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PH DOMAIN OF HUMAN DOCKING PROTEIN
JRNL TITL 2 BRDG1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X1F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000024257.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.00MM PH DOMAIN U-13C, 15N;
REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.913, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LEAST 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 O LYS A 129 H VAL A 133 1.51
REMARK 500 O LEU A 46 H LEU A 61 1.53
REMARK 500 O TRP A 104 H ILE A 108 1.55
REMARK 500 H THR A 67 O VAL A 85 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 THR A 14 -69.22 -122.43
REMARK 500 1 ALA A 15 -60.85 -146.63
REMARK 500 1 PHE A 23 108.25 -55.85
REMARK 500 1 SER A 29 112.37 -39.58
REMARK 500 1 ARG A 32 -46.18 84.74
REMARK 500 1 TYR A 34 130.10 -36.32
REMARK 500 1 THR A 44 19.16 -146.82
REMARK 500 1 LEU A 61 -161.91 -120.54
REMARK 500 1 CYS A 68 -179.81 167.94
REMARK 500 1 SER A 74 88.21 49.10
REMARK 500 1 GLU A 76 -59.34 -169.74
REMARK 500 1 THR A 95 -161.61 -122.41
REMARK 500 1 THR A 112 -48.84 -143.47
REMARK 500 1 SER A 115 -156.64 -141.90
REMARK 500 1 ASN A 119 57.23 -109.85
REMARK 500 1 LEU A 122 -176.99 -56.19
REMARK 500 1 ILE A 142 -79.62 -43.27
REMARK 500 1 SER A 144 -53.57 -124.53
REMARK 500 1 SER A 148 163.44 64.43
REMARK 500 2 SER A 2 169.17 179.77
REMARK 500 2 SER A 5 89.75 61.64
REMARK 500 2 SER A 6 111.17 -170.99
REMARK 500 2 GLN A 8 76.20 46.74
REMARK 500 2 LEU A 11 105.77 64.81
REMARK 500 2 PHE A 20 144.94 -176.79
REMARK 500 2 PHE A 23 99.60 -44.11
REMARK 500 2 ARG A 28 -80.89 -40.98
REMARK 500 2 SER A 29 -55.74 -161.28
REMARK 500 2 GLU A 33 148.25 -178.13
REMARK 500 2 TYR A 34 123.94 -37.49
REMARK 500 2 TRP A 38 87.89 -65.81
REMARK 500 2 THR A 44 20.21 -150.16
REMARK 500 2 CYS A 68 -179.32 164.44
REMARK 500 2 SER A 74 -59.16 179.93
REMARK 500 2 GLU A 76 173.25 -50.12
REMARK 500 2 ASN A 78 -49.54 178.20
REMARK 500 2 THR A 112 -45.18 -147.92
REMARK 500 2 GLN A 118 30.78 -90.85
REMARK 500 2 LEU A 122 -179.34 -50.95
REMARK 500 2 ILE A 142 -78.97 -43.27
REMARK 500 3 SER A 2 97.05 -175.30
REMARK 500 3 SER A 6 -57.84 -121.98
REMARK 500 3 ILE A 13 142.41 65.21
REMARK 500 3 PHE A 20 144.08 -176.09
REMARK 500 3 PHE A 23 98.91 -37.53
REMARK 500 3 SER A 29 90.90 -65.41
REMARK 500 3 CYS A 68 -178.65 -179.11
REMARK 500 3 SER A 74 -61.21 -140.70
REMARK 500 3 THR A 75 121.57 62.90
REMARK 500 3 GLU A 76 -58.47 72.44
REMARK 500
REMARK 500 THIS ENTRY HAS 444 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001002916.1 RELATED DB: TARGETDB
DBREF 1X1F A 8 143 UNP Q9ULZ2 STAP1_HUMAN 16 151
SEQADV 1X1F GLY A 1 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F SER A 2 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F SER A 3 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F GLY A 4 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F SER A 5 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F SER A 6 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F GLY A 7 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F SER A 144 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F GLY A 145 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F PRO A 146 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F SER A 147 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F SER A 148 UNP Q9ULZ2 CLONING ARTIFACT
SEQADV 1X1F GLY A 149 UNP Q9ULZ2 CLONING ARTIFACT
SEQRES 1 A 149 GLY SER SER GLY SER SER GLY GLN GLU ARG LEU LYS ILE
SEQRES 2 A 149 THR ALA LEU PRO LEU TYR PHE GLU GLY PHE LEU LEU ILE
SEQRES 3 A 149 LYS ARG SER GLY TYR ARG GLU TYR GLU HIS TYR TRP THR
SEQRES 4 A 149 GLU LEU ARG GLY THR THR LEU PHE PHE TYR THR ASP LYS
SEQRES 5 A 149 LYS SER ILE ILE TYR VAL ASP LYS LEU ASP ILE VAL ASP
SEQRES 6 A 149 LEU THR CYS LEU THR GLU GLN ASN SER THR GLU LYS ASN
SEQRES 7 A 149 CYS ALA LYS PHE THR LEU VAL LEU PRO LYS GLU GLU VAL
SEQRES 8 A 149 GLN LEU LYS THR GLU ASN THR GLU SER GLY GLU GLU TRP
SEQRES 9 A 149 ARG GLY PHE ILE LEU THR VAL THR GLU LEU SER VAL PRO
SEQRES 10 A 149 GLN ASN VAL SER LEU LEU PRO GLY GLN VAL ILE LYS LEU
SEQRES 11 A 149 HIS GLU VAL LEU GLU ARG GLU LYS LYS ARG ARG ILE GLU
SEQRES 12 A 149 SER GLY PRO SER SER GLY
HELIX 1 1 THR A 98 GLU A 113 1 16
HELIX 2 2 PRO A 124 ILE A 142 1 19
SHEET 1 A 7 ASP A 59 ASP A 62 0
SHEET 2 A 7 THR A 45 TYR A 49 -1 N PHE A 48 O ASP A 59
SHEET 3 A 7 GLU A 35 ARG A 42 -1 N ARG A 42 O THR A 45
SHEET 4 A 7 LEU A 18 LYS A 27 -1 N ILE A 26 O GLU A 35
SHEET 5 A 7 VAL A 91 LYS A 94 -1 O GLN A 92 N LYS A 27
SHEET 6 A 7 LYS A 81 VAL A 85 -1 N LEU A 84 O VAL A 91
SHEET 7 A 7 CYS A 68 GLU A 71 -1 N CYS A 68 O VAL A 85
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