Header list of 2d8k.pdb file
Complete list - r 9 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 06-DEC-05 2D8K
TITLE SOLUTION STRUCTURE OF THE FIRST C2 DOMAIN OF SYNAPTOTAGMIN VII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPTOTAGMIN VII;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2 DOMAIN;
COMPND 5 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: SYT7;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050620-09;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS EXOCYTOSIS, CALCIUM BINDING, LYSOSOME, C2 DOMAIN, SYNAPTOTAGMIN,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D8K 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D8K 1 VERSN
REVDAT 1 06-JUN-06 2D8K 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST C2 DOMAIN OF SYNAPTOTAGMIN
JRNL TITL 2 VII
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D8K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025121.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.20MM C2 DOMAIN U-15N,13C; 20MM
REMARK 210 TRISHCL, 100MM NACL, 1MM DTT,
REMARK 210 0.02% NAN3; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.901, CYANA 2.0.17
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 LOWEST ENERGY
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 MET A 33 -75.30 -40.78
REMARK 500 1 LYS A 34 -178.77 -174.89
REMARK 500 1 LYS A 41 -39.45 -131.61
REMARK 500 1 ASP A 48 79.43 -108.32
REMARK 500 1 ASP A 58 126.63 -33.28
REMARK 500 1 LYS A 66 178.97 -56.95
REMARK 500 1 ASN A 77 35.01 34.47
REMARK 500 1 LYS A 89 -60.17 -99.55
REMARK 500 1 VAL A 90 -30.50 -38.48
REMARK 500 1 TYR A 102 105.64 -57.76
REMARK 500 1 ASN A 108 119.65 -163.91
REMARK 500 1 ASP A 122 78.07 -62.63
REMARK 500 1 LEU A 133 99.36 -34.54
REMARK 500 1 PRO A 135 95.57 -69.70
REMARK 500 1 PRO A 138 -173.38 -69.72
REMARK 500 2 ASN A 11 52.72 -97.24
REMARK 500 2 MET A 33 -75.90 -47.07
REMARK 500 2 SER A 44 -70.81 -35.52
REMARK 500 2 ASP A 58 96.55 -33.73
REMARK 500 2 LYS A 60 -62.41 -95.14
REMARK 500 2 ASN A 77 33.63 34.78
REMARK 500 2 ARG A 107 104.30 -38.88
REMARK 500 2 ASP A 122 81.84 -68.85
REMARK 500 2 LEU A 133 102.24 -42.47
REMARK 500 3 ASN A 11 74.54 -68.23
REMARK 500 3 MET A 33 -74.63 -44.03
REMARK 500 3 LYS A 34 -176.05 -174.70
REMARK 500 3 ASP A 48 69.96 -108.42
REMARK 500 3 ASP A 58 128.89 -33.48
REMARK 500 3 ASN A 77 33.18 35.14
REMARK 500 3 ASP A 122 91.01 -67.53
REMARK 500 3 LEU A 133 108.61 -37.20
REMARK 500 3 PRO A 135 96.86 -69.73
REMARK 500 4 ASN A 11 45.54 -83.39
REMARK 500 4 PHE A 23 -70.70 -83.70
REMARK 500 4 MET A 33 -75.92 -36.32
REMARK 500 4 ASP A 48 78.56 -110.86
REMARK 500 4 ASP A 58 126.69 -33.77
REMARK 500 4 LYS A 66 170.51 -46.32
REMARK 500 4 ASN A 73 50.75 -117.72
REMARK 500 4 VAL A 90 -37.10 -34.96
REMARK 500 4 THR A 124 -29.61 -36.88
REMARK 500 4 LEU A 133 99.63 -34.17
REMARK 500 5 SER A 5 152.12 -49.96
REMARK 500 5 ASN A 11 77.94 -67.32
REMARK 500 5 MET A 33 -75.84 -46.27
REMARK 500 5 LYS A 34 -179.48 -171.18
REMARK 500 5 LYS A 41 47.59 -86.41
REMARK 500 5 ASP A 42 116.07 -172.63
REMARK 500 5 ASP A 58 125.06 -32.49
REMARK 500
REMARK 500 THIS ENTRY HAS 241 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002002479.1 RELATED DB: TARGETDB
DBREF 2D8K A 8 135 GB 38570146 NP_004191 132 259
SEQADV 2D8K GLY A 1 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K SER A 2 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K SER A 3 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K GLY A 4 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K SER A 5 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K SER A 6 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K GLY A 7 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K SER A 136 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K GLY A 137 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K PRO A 138 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K SER A 139 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K SER A 140 GB 38570146 CLONING ARTIFACT
SEQADV 2D8K GLY A 141 GB 38570146 CLONING ARTIFACT
SEQRES 1 A 141 GLY SER SER GLY SER SER GLY SER ARG GLU ASN LEU GLY
SEQRES 2 A 141 ARG ILE GLN PHE SER VAL GLY TYR ASN PHE GLN GLU SER
SEQRES 3 A 141 THR LEU THR VAL LYS ILE MET LYS ALA GLN GLU LEU PRO
SEQRES 4 A 141 ALA LYS ASP PHE SER GLY THR SER ASP PRO PHE VAL LYS
SEQRES 5 A 141 ILE TYR LEU LEU PRO ASP LYS LYS HIS LYS LEU GLU THR
SEQRES 6 A 141 LYS VAL LYS ARG LYS ASN LEU ASN PRO HIS TRP ASN GLU
SEQRES 7 A 141 THR PHE LEU PHE GLU GLY PHE PRO TYR GLU LYS VAL VAL
SEQRES 8 A 141 GLN ARG ILE LEU TYR LEU GLN VAL LEU ASP TYR ASP ARG
SEQRES 9 A 141 PHE SER ARG ASN ASP PRO ILE GLY GLU VAL SER ILE PRO
SEQRES 10 A 141 LEU ASN LYS VAL ASP LEU THR GLN MET GLN THR PHE TRP
SEQRES 11 A 141 LYS ASP LEU LYS PRO SER GLY PRO SER SER GLY
HELIX 1 1 PRO A 86 VAL A 91 1 6
SHEET 1 A 4 GLU A 78 PHE A 82 0
SHEET 2 A 4 LEU A 28 GLN A 36 -1 N ILE A 32 O GLU A 78
SHEET 3 A 4 ARG A 14 TYR A 21 -1 N SER A 18 O LYS A 31
SHEET 4 A 4 GLN A 127 LYS A 131 -1 O GLN A 127 N VAL A 19
SHEET 1 B 5 LYS A 62 GLU A 64 0
SHEET 2 B 5 PRO A 49 LEU A 56 -1 N ILE A 53 O LEU A 63
SHEET 3 B 5 ILE A 94 ASP A 101 -1 O LEU A 100 N PHE A 50
SHEET 4 B 5 ASP A 109 PRO A 117 -1 O ILE A 116 N LEU A 95
SHEET 5 B 5 LYS A 134 PRO A 135 -1 O LYS A 134 N GLU A 113
CISPEP 1 LEU A 56 PRO A 57 1 -0.10
CISPEP 2 LEU A 56 PRO A 57 2 -0.12
CISPEP 3 LEU A 56 PRO A 57 3 -0.15
CISPEP 4 LEU A 56 PRO A 57 4 -0.12
CISPEP 5 LEU A 56 PRO A 57 5 -0.07
CISPEP 6 LEU A 56 PRO A 57 6 -0.14
CISPEP 7 LEU A 56 PRO A 57 7 -0.11
CISPEP 8 LEU A 56 PRO A 57 8 -0.12
CISPEP 9 LEU A 56 PRO A 57 9 -0.19
CISPEP 10 LEU A 56 PRO A 57 10 -0.09
CISPEP 11 LEU A 56 PRO A 57 11 -0.16
CISPEP 12 LEU A 56 PRO A 57 12 -0.18
CISPEP 13 LEU A 56 PRO A 57 13 -0.05
CISPEP 14 LEU A 56 PRO A 57 14 -0.06
CISPEP 15 LEU A 56 PRO A 57 15 -0.12
CISPEP 16 LEU A 56 PRO A 57 16 -0.17
CISPEP 17 LEU A 56 PRO A 57 17 -0.15
CISPEP 18 LEU A 56 PRO A 57 18 -0.14
CISPEP 19 LEU A 56 PRO A 57 19 -0.20
CISPEP 20 LEU A 56 PRO A 57 20 -0.19
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 9 2 Bytes