Header list of 1x05.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 15-MAR-05 1X05
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL PH DOMAIN OF HUMAN PLECKSTRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLECKSTRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PH DOMAIN;
COMPND 5 SYNONYM: PLATELET P47 PROTEIN;
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_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P040517-04;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PLECKSTRIN, PH DOMAIN, STRUCTURAL GENOMICS, NPPSFA, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, SIGNALING 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 1X05 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X05 1 VERSN
REVDAT 1 15-SEP-05 1X05 0
JRNL AUTH H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL PH DOMAIN OF HUMAN
JRNL TITL 2 PLECKSTRIN
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 1X05 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000024212.
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 : 120 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.13MM 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 H VAL A 69 O ILE A 91 1.51
REMARK 500 OE2 GLU A 89 HD1 HIS A 97 1.53
REMARK 500 H ILE A 40 O HIS A 49 1.53
REMARK 500 O GLU A 110 H ALA A 114 1.57
REMARK 500 O ALA A 118 H THR A 121 1.59
REMARK 500 H LEU A 24 O ARG A 37 1.60
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 SER A 6 75.14 51.40
REMARK 500 1 ILE A 9 154.28 -45.62
REMARK 500 1 LYS A 11 -168.28 -55.43
REMARK 500 1 ASN A 33 166.76 58.00
REMARK 500 1 ASP A 44 75.81 56.75
REMARK 500 1 ALA A 56 -175.54 62.15
REMARK 500 1 GLU A 57 -55.25 -137.74
REMARK 500 1 SER A 75 80.30 40.41
REMARK 500 1 SER A 77 98.21 59.19
REMARK 500 1 LYS A 81 -62.03 77.04
REMARK 500 1 SER A 82 82.66 62.84
REMARK 500 1 ASN A 86 86.70 58.03
REMARK 500 1 GLU A 95 0.20 80.93
REMARK 500 1 THR A 121 -168.05 43.76
REMARK 500 1 LYS A 123 -179.34 67.40
REMARK 500 1 SER A 124 99.42 52.78
REMARK 500 1 SER A 127 -68.43 74.68
REMARK 500 1 SER A 128 114.53 63.54
REMARK 500 2 ILE A 9 156.87 -41.40
REMARK 500 2 LYS A 11 -168.11 -55.76
REMARK 500 2 GLN A 27 141.91 -37.78
REMARK 500 2 HIS A 29 79.47 -63.31
REMARK 500 2 ARG A 31 -42.76 177.39
REMARK 500 2 ASN A 33 -173.71 -53.65
REMARK 500 2 TRP A 34 -167.97 -59.64
REMARK 500 2 ASP A 44 76.65 57.49
REMARK 500 2 ALA A 56 -178.94 178.93
REMARK 500 2 GLU A 57 -63.65 -122.53
REMARK 500 2 VAL A 73 -162.28 -70.71
REMARK 500 2 ASN A 76 103.82 -162.59
REMARK 500 2 SER A 77 143.73 177.34
REMARK 500 2 ARG A 80 -62.26 -98.95
REMARK 500 2 LYS A 81 -177.98 -70.00
REMARK 500 2 GLU A 85 -148.30 -77.47
REMARK 500 2 GLU A 95 3.65 81.17
REMARK 500 2 THR A 121 -167.70 45.78
REMARK 500 2 SER A 124 84.81 177.81
REMARK 500 2 SER A 127 169.18 70.79
REMARK 500 2 SER A 128 106.84 66.87
REMARK 500 3 SER A 2 157.27 60.27
REMARK 500 3 SER A 3 -55.24 -146.80
REMARK 500 3 SER A 6 -51.91 -140.29
REMARK 500 3 VAL A 8 161.09 58.56
REMARK 500 3 LYS A 11 -164.65 -59.48
REMARK 500 3 PHE A 14 35.55 -97.73
REMARK 500 3 HIS A 29 -60.72 -131.98
REMARK 500 3 ASP A 44 75.93 57.77
REMARK 500 3 ALA A 56 -173.94 179.90
REMARK 500 3 GLU A 57 -62.06 -136.03
REMARK 500 3 ASN A 78 142.50 177.12
REMARK 500
REMARK 500 THIS ENTRY HAS 367 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: HSS001003763.1 RELATED DB: TARGETDB
DBREF 1X05 A 8 123 UNP P08567 PLEK_HUMAN 235 350
SEQADV 1X05 GLY A 1 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 SER A 2 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 SER A 3 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 GLY A 4 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 SER A 5 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 SER A 6 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 GLY A 7 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 SER A 124 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 GLY A 125 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 PRO A 126 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 SER A 127 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 SER A 128 UNP P08567 CLONING ARTIFACT
SEQADV 1X05 GLY A 129 UNP P08567 CLONING ARTIFACT
SEQRES 1 A 129 GLY SER SER GLY SER SER GLY VAL ILE LEU LYS GLU GLU
SEQRES 2 A 129 PHE ARG GLY VAL ILE ILE LYS GLN GLY CYS LEU LEU LYS
SEQRES 3 A 129 GLN GLY HIS ARG ARG LYS ASN TRP LYS VAL ARG LYS PHE
SEQRES 4 A 129 ILE LEU ARG GLU ASP PRO ALA TYR LEU HIS TYR TYR ASP
SEQRES 5 A 129 PRO ALA GLY ALA GLU ASP PRO LEU GLY ALA ILE HIS LEU
SEQRES 6 A 129 ARG GLY CYS VAL VAL THR SER VAL GLU SER ASN SER ASN
SEQRES 7 A 129 GLY ARG LYS SER GLU GLU GLU ASN LEU PHE GLU ILE ILE
SEQRES 8 A 129 THR ALA ASP GLU VAL HIS TYR PHE LEU GLN ALA ALA THR
SEQRES 9 A 129 PRO LYS GLU ARG THR GLU TRP ILE LYS ALA ILE GLN MET
SEQRES 10 A 129 ALA SER ARG THR GLY LYS SER GLY PRO SER SER GLY
HELIX 1 1 LYS A 106 ARG A 120 1 15
SHEET 1 A 4 VAL A 17 LYS A 26 0
SHEET 2 A 4 LYS A 35 GLU A 43 -1 O ARG A 37 N LEU A 24
SHEET 3 A 4 TYR A 47 TYR A 51 -1 O HIS A 49 N ILE A 40
SHEET 4 A 4 GLY A 61 HIS A 64 -1 O ILE A 63 N LEU A 48
SHEET 1 B 3 VAL A 69 SER A 72 0
SHEET 2 B 3 LEU A 87 ILE A 91 -1 O ILE A 91 N VAL A 69
SHEET 3 B 3 HIS A 97 GLN A 101 -1 O LEU A 100 N PHE A 88
CISPEP 1 ASP A 44 PRO A 45 1 -0.02
CISPEP 2 ASP A 44 PRO A 45 2 -0.01
CISPEP 3 ASP A 44 PRO A 45 3 0.01
CISPEP 4 ASP A 44 PRO A 45 4 0.06
CISPEP 5 ASP A 44 PRO A 45 5 -0.01
CISPEP 6 ASP A 44 PRO A 45 6 -0.08
CISPEP 7 ASP A 44 PRO A 45 7 0.01
CISPEP 8 ASP A 44 PRO A 45 8 0.02
CISPEP 9 ASP A 44 PRO A 45 9 -0.05
CISPEP 10 ASP A 44 PRO A 45 10 -0.09
CISPEP 11 ASP A 44 PRO A 45 11 0.01
CISPEP 12 ASP A 44 PRO A 45 12 0.01
CISPEP 13 ASP A 44 PRO A 45 13 -0.05
CISPEP 14 ASP A 44 PRO A 45 14 0.04
CISPEP 15 ASP A 44 PRO A 45 15 -0.04
CISPEP 16 ASP A 44 PRO A 45 16 0.02
CISPEP 17 ASP A 44 PRO A 45 17 -0.03
CISPEP 18 ASP A 44 PRO A 45 18 0.00
CISPEP 19 ASP A 44 PRO A 45 19 0.06
CISPEP 20 ASP A 44 PRO A 45 20 0.02
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