Header list of 1v27.pdb file
Complete list - r 2 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 07-OCT-03 1V27
TITLE SOLUTION STRUCTURE OF THE FIRST C2 DOMAIN OF RIM2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2 DOMAIN;
COMPND 5 SYNONYM: RAB3-INTERACTING MOLECULE 2, RIM2;
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 KIAA0751;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020930-02;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS C2, EXOCYTOSIS, RAB3-INTERACTING MOLECULE, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS,
KEYWDS 3 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 02-MAR-22 1V27 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V27 1 VERSN
REVDAT 1 07-APR-04 1V27 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST C2 DOMAIN OF RIM2
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 1.0.7
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V27 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000006113.
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 : 1.1MM 13C/15N-LABELED PROTEIN;
REMARK 210 20MM TRIS-D11, 100MM NACL, 0.02%
REMARK 210 NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 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 0.861, 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 : 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: 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 HIS A 21 H VAL A 82 1.52
REMARK 500 O ILE A 94 H ILE A 113 1.52
REMARK 500 H LEU A 23 O TYR A 79 1.54
REMARK 500 O TRP A 15 H ILE A 24 1.58
REMARK 500 O LYS A 13 H THR A 26 1.58
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 2 92.04 64.44
REMARK 500 1 VAL A 19 -72.73 -55.14
REMARK 500 1 LEU A 28 -99.95 -55.41
REMARK 500 1 SER A 35 -168.32 -108.31
REMARK 500 1 GLU A 37 -88.28 -96.90
REMARK 500 1 ASP A 38 56.89 -106.96
REMARK 500 1 PRO A 41 -162.07 -75.06
REMARK 500 1 PRO A 52 -169.44 -75.00
REMARK 500 1 ASP A 53 128.75 78.98
REMARK 500 1 SER A 55 -51.12 -161.69
REMARK 500 1 ASP A 56 -160.75 -179.67
REMARK 500 1 LYS A 57 -82.68 76.79
REMARK 500 1 ASN A 58 36.97 -94.70
REMARK 500 1 LYS A 67 89.36 41.05
REMARK 500 1 THR A 68 111.23 -178.08
REMARK 500 1 ASN A 74 36.84 38.47
REMARK 500 1 ALA A 100 -82.84 -67.34
REMARK 500 1 ARG A 101 177.17 -57.48
REMARK 500 1 PHE A 109 111.13 55.54
REMARK 500 1 ASP A 123 23.73 -151.98
REMARK 500 1 ASP A 135 152.36 -49.41
REMARK 500 1 SER A 136 110.68 66.69
REMARK 500 1 SER A 139 127.57 -179.42
REMARK 500 2 SER A 3 93.95 -170.43
REMARK 500 2 SER A 5 132.62 179.53
REMARK 500 2 VAL A 19 -71.92 -51.66
REMARK 500 2 LEU A 28 -98.87 -58.10
REMARK 500 2 ARG A 36 77.41 -111.47
REMARK 500 2 GLU A 37 174.44 52.16
REMARK 500 2 PRO A 41 -162.33 -74.98
REMARK 500 2 PHE A 50 96.41 -68.30
REMARK 500 2 ASP A 53 166.60 60.24
REMARK 500 2 ARG A 54 94.88 -160.67
REMARK 500 2 LYS A 67 87.47 50.78
REMARK 500 2 THR A 68 113.28 -177.69
REMARK 500 2 ASN A 74 37.03 38.31
REMARK 500 2 GLN A 99 82.83 -69.43
REMARK 500 2 ARG A 101 163.31 57.10
REMARK 500 2 ARG A 103 58.95 -110.29
REMARK 500 2 GLU A 106 64.74 38.84
REMARK 500 2 PHE A 109 102.63 51.51
REMARK 500 2 LEU A 121 93.33 -67.84
REMARK 500 2 ASP A 123 26.00 -158.17
REMARK 500 2 HIS A 134 131.48 -175.70
REMARK 500 2 SER A 136 149.58 -171.89
REMARK 500 2 SER A 140 105.57 59.11
REMARK 500 3 SER A 2 163.17 -46.56
REMARK 500 3 SER A 3 -49.33 -165.16
REMARK 500 3 SER A 6 135.80 -176.99
REMARK 500 3 VAL A 19 -71.01 -54.92
REMARK 500
REMARK 500 THIS ENTRY HAS 482 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000733.2 RELATED DB: TARGETDB
DBREF 1V27 A 8 135 UNP Q9UQ26 RIMS2_HUMAN 584 711
SEQADV 1V27 GLY A 1 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 SER A 2 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 SER A 3 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 GLY A 4 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 SER A 5 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 SER A 6 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 GLY A 7 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 SER A 136 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 GLY A 137 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 PRO A 138 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 SER A 139 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 SER A 140 UNP Q9UQ26 CLONING ARTIFACT
SEQADV 1V27 GLY A 141 UNP Q9UQ26 CLONING ARTIFACT
SEQRES 1 A 141 GLY SER SER GLY SER SER GLY GLY GLN LEU SER ILE LYS
SEQRES 2 A 141 LEU TRP PHE ASP LYS VAL GLY HIS GLN LEU ILE VAL THR
SEQRES 3 A 141 ILE LEU GLY ALA LYS ASP LEU PRO SER ARG GLU ASP GLY
SEQRES 4 A 141 ARG PRO ARG ASN PRO TYR VAL LYS ILE TYR PHE LEU PRO
SEQRES 5 A 141 ASP ARG SER ASP LYS ASN LYS ARG ARG THR LYS THR VAL
SEQRES 6 A 141 LYS LYS THR LEU GLU PRO LYS TRP ASN GLN THR PHE ILE
SEQRES 7 A 141 TYR SER PRO VAL HIS ARG ARG GLU PHE ARG GLU ARG MET
SEQRES 8 A 141 LEU GLU ILE THR LEU TRP ASP GLN ALA ARG VAL ARG GLU
SEQRES 9 A 141 GLU GLU SER GLU PHE LEU GLY GLU ILE LEU ILE GLU LEU
SEQRES 10 A 141 GLU THR ALA LEU LEU ASP ASP GLU PRO HIS TRP TYR LYS
SEQRES 11 A 141 LEU GLN THR HIS ASP SER GLY PRO SER SER GLY
HELIX 1 1 ARG A 85 GLU A 89 5 5
HELIX 2 2 GLU A 118 ALA A 120 5 3
SHEET 1 A 4 ILE A 78 TYR A 79 0
SHEET 2 A 4 GLN A 22 LYS A 31 -1 N LEU A 23 O TYR A 79
SHEET 3 A 4 GLN A 9 ASP A 17 -1 N LYS A 13 O THR A 26
SHEET 4 A 4 PRO A 126 LYS A 130 -1 O TYR A 129 N LEU A 10
SHEET 1 B 3 PRO A 44 LYS A 47 0
SHEET 2 B 3 MET A 91 ASP A 98 -1 O TRP A 97 N TYR A 45
SHEET 3 B 3 GLY A 111 GLU A 116 -1 O ILE A 113 N ILE A 94
CISPEP 1 LEU A 51 PRO A 52 1 -0.02
CISPEP 2 SER A 80 PRO A 81 1 0.03
CISPEP 3 LEU A 51 PRO A 52 2 -0.03
CISPEP 4 SER A 80 PRO A 81 2 0.03
CISPEP 5 LEU A 51 PRO A 52 3 0.07
CISPEP 6 SER A 80 PRO A 81 3 -0.07
CISPEP 7 LEU A 51 PRO A 52 4 -0.08
CISPEP 8 SER A 80 PRO A 81 4 -0.03
CISPEP 9 LEU A 51 PRO A 52 5 -0.03
CISPEP 10 SER A 80 PRO A 81 5 -0.08
CISPEP 11 LEU A 51 PRO A 52 6 0.03
CISPEP 12 SER A 80 PRO A 81 6 0.00
CISPEP 13 LEU A 51 PRO A 52 7 -0.05
CISPEP 14 SER A 80 PRO A 81 7 -0.06
CISPEP 15 LEU A 51 PRO A 52 8 -0.04
CISPEP 16 SER A 80 PRO A 81 8 0.03
CISPEP 17 LEU A 51 PRO A 52 9 -0.01
CISPEP 18 SER A 80 PRO A 81 9 0.07
CISPEP 19 LEU A 51 PRO A 52 10 -0.03
CISPEP 20 SER A 80 PRO A 81 10 0.02
CISPEP 21 LEU A 51 PRO A 52 11 0.11
CISPEP 22 SER A 80 PRO A 81 11 0.07
CISPEP 23 LEU A 51 PRO A 52 12 -0.02
CISPEP 24 SER A 80 PRO A 81 12 0.08
CISPEP 25 LEU A 51 PRO A 52 13 -0.04
CISPEP 26 SER A 80 PRO A 81 13 -0.02
CISPEP 27 LEU A 51 PRO A 52 14 0.02
CISPEP 28 SER A 80 PRO A 81 14 0.06
CISPEP 29 LEU A 51 PRO A 52 15 0.04
CISPEP 30 SER A 80 PRO A 81 15 0.03
CISPEP 31 LEU A 51 PRO A 52 16 -0.04
CISPEP 32 SER A 80 PRO A 81 16 0.02
CISPEP 33 LEU A 51 PRO A 52 17 0.08
CISPEP 34 SER A 80 PRO A 81 17 0.01
CISPEP 35 LEU A 51 PRO A 52 18 0.06
CISPEP 36 SER A 80 PRO A 81 18 -0.04
CISPEP 37 LEU A 51 PRO A 52 19 0.03
CISPEP 38 SER A 80 PRO A 81 19 -0.03
CISPEP 39 LEU A 51 PRO A 52 20 -0.04
CISPEP 40 SER A 80 PRO A 81 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