Header list of 1wi1.pdb file
Complete list - r 2 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 28-MAY-04 1WI1
TITLE SOLUTION STRUCTURE OF THE PH DOMAIN OF HUMAN CALCIUM-DEPENDENT
TITLE 2 ACTIVATOR PROTEIN FOR SECRETION (CAPS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM-DEPENDENT ACTIVATOR PROTEIN FOR SECRETION, CAPS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PH DOMAIN;
COMPND 5 SYNONYM: KIAA1121 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 GENE: KAZUSA CDNA HH10147;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030428-81;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PH DOMAIN, CALCIUM-DEPENDENT ACTIVATOR PROTEIN FOR SECRETION (CAPS),
KEYWDS 2 PIP2 BINDING SITE, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,K.IZUMI,M.YOSHIDA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WI1 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WI1 1 VERSN
REVDAT 1 28-NOV-04 1WI1 0
JRNL AUTH M.YONEYAMA,K.IZUMI,M.YOSHIDA,N.TOCHIO,S.KOSHIBA,M.INOUE,
JRNL AUTH 2 T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PH DOMAIN OF HUMAN
JRNL TITL 2 CALCIUM-DEPENDENT ACTIVATOR PROTEIN FOR SECRETION (CAPS)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 20020425, CYANA 2.0.17
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WI1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023600.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 297
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PH DOMAIN U-15N, 13C; 20MM
REMARK 210 PINA; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3; 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 : ECA
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, KUJIRA 0.896,
REMARK 210 CYANA 2.0.17, DELTA 2.3
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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 FUNCTION
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: 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 LYS A 23 -38.45 -38.34
REMARK 500 1 LYS A 49 48.38 71.83
REMARK 500 1 LEU A 58 31.14 -85.09
REMARK 500 1 TYR A 61 135.61 -37.43
REMARK 500 1 LEU A 72 106.82 -56.28
REMARK 500 1 GLU A 73 64.34 -119.63
REMARK 500 1 PRO A 118 -175.14 -69.71
REMARK 500 2 PRO A 52 99.44 -69.74
REMARK 500 2 LEU A 58 33.92 -85.78
REMARK 500 2 GLU A 73 72.48 -113.70
REMARK 500 2 ARG A 76 -60.55 -90.74
REMARK 500 2 GLN A 111 177.19 -50.50
REMARK 500 2 GLN A 120 105.65 -49.69
REMARK 500 2 SER A 125 -60.24 -122.08
REMARK 500 3 SER A 5 151.93 -43.72
REMARK 500 3 GLN A 53 -72.51 -79.27
REMARK 500 3 LEU A 58 33.87 -98.01
REMARK 500 3 TYR A 61 141.25 -34.53
REMARK 500 3 PRO A 70 89.10 -69.71
REMARK 500 3 ARG A 76 -69.42 -92.66
REMARK 500 3 GLN A 111 -178.48 -56.66
REMARK 500 3 PRO A 118 -177.08 -69.79
REMARK 500 3 PRO A 123 84.97 -69.73
REMARK 500 4 SER A 3 151.99 -35.26
REMARK 500 4 TRP A 22 28.91 47.64
REMARK 500 4 ALA A 50 132.44 -34.09
REMARK 500 4 PRO A 52 93.24 -69.73
REMARK 500 4 LEU A 58 38.36 -96.68
REMARK 500 4 ASP A 64 149.88 -171.70
REMARK 500 4 GLN A 111 177.81 -51.81
REMARK 500 5 TRP A 22 38.32 37.87
REMARK 500 5 PHE A 29 98.74 -69.33
REMARK 500 5 PRO A 52 95.47 -69.80
REMARK 500 5 LEU A 58 35.33 -93.43
REMARK 500 5 ASP A 59 43.38 -79.95
REMARK 500 5 TYR A 61 144.10 -39.15
REMARK 500 5 LEU A 72 102.05 -36.03
REMARK 500 5 GLN A 111 174.89 -59.97
REMARK 500 5 PRO A 118 -176.24 -69.82
REMARK 500 5 THR A 119 137.93 -174.46
REMARK 500 5 SER A 121 111.51 -174.87
REMARK 500 5 SER A 124 130.28 -172.62
REMARK 500 6 MET A 8 133.03 -38.47
REMARK 500 6 LYS A 23 -31.60 -39.83
REMARK 500 6 LYS A 49 60.63 -111.13
REMARK 500 6 PRO A 52 91.86 -69.72
REMARK 500 6 PRO A 68 96.59 -69.79
REMARK 500 6 PRO A 70 96.08 -69.77
REMARK 500 6 GLU A 73 64.36 -109.45
REMARK 500 6 GLN A 111 -177.45 -54.48
REMARK 500
REMARK 500 THIS ENTRY HAS 159 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002101095.1 RELATED DB: TARGETDB
DBREF 1WI1 A 8 120 UNP Q8NFR0 Q8NFR0_HUMAN 559 671
SEQADV 1WI1 GLY A 1 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 SER A 2 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 SER A 3 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 GLY A 4 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 SER A 5 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 SER A 6 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 GLY A 7 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 SER A 121 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 GLY A 122 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 PRO A 123 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 SER A 124 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 SER A 125 UNP Q8NFR0 CLONING ARTIFACT
SEQADV 1WI1 GLY A 126 UNP Q8NFR0 CLONING ARTIFACT
SEQRES 1 A 126 GLY SER SER GLY SER SER GLY MET LYS HIS SER GLY TYR
SEQRES 2 A 126 LEU TRP ALA ILE GLY LYS ASN VAL TRP LYS ARG TRP LYS
SEQRES 3 A 126 LYS ARG PHE PHE VAL LEU VAL GLN VAL SER GLN TYR THR
SEQRES 4 A 126 PHE ALA MET CYS SER TYR ARG GLU LYS LYS ALA GLU PRO
SEQRES 5 A 126 GLN GLU LEU LEU GLN LEU ASP GLY TYR THR VAL ASP TYR
SEQRES 6 A 126 THR ASP PRO GLN PRO GLY LEU GLU GLY GLY ARG ALA PHE
SEQRES 7 A 126 PHE ASN ALA VAL LYS GLU GLY ASP THR VAL ILE PHE ALA
SEQRES 8 A 126 SER ASP ASP GLU GLN ASP ARG ILE LEU TRP VAL GLN ALA
SEQRES 9 A 126 MET TYR ARG ALA THR GLY GLN SER HIS LYS PRO VAL PRO
SEQRES 10 A 126 PRO THR GLN SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 94 GLY A 110 1 17
SHEET 1 A 7 LEU A 55 GLN A 57 0
SHEET 2 A 7 THR A 39 CYS A 43 -1
SHEET 3 A 7 LYS A 26 SER A 36 -1
SHEET 4 A 7 SER A 11 ILE A 17 -1
SHEET 5 A 7 THR A 87 ALA A 91 -1
SHEET 6 A 7 PHE A 78 VAL A 82 -1
SHEET 7 A 7 THR A 62 TYR A 65 -1
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