Header list of 1wfm.pdb file
Complete list - r 2 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 26-MAY-04 1WFM
TITLE THE FIRST C2 DOMAIN OF HUMAN SYNAPTOTAGMIN XIII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPTOTAGMIN XIII;
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: KAZUSA CDNA FH02770;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040113-87;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS C2 DOMAIN, EXOCYTOSIS, NEUROTRANSMITTER RELEASE, 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 1WFM 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WFM 1 VERSN
REVDAT 1 26-NOV-04 1WFM 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL THE FIRST C2 DOMAIN OF HUMAN SYNAPTOTAGMIN XIII
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 1WFM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023525.
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 : 1.07MM 13C/15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS, 100MM NACL, 5MM D-
REMARK 210 DTT, 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 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 0.8992, 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 LYS A 14 H VAL A 36 1.51
REMARK 500 O ALA A 83 H GLU A 86 1.53
REMARK 500 O LEU A 94 H LEU A 111 1.55
REMARK 500 O GLU A 110 H LYS A 131 1.57
REMARK 500 H LEU A 28 O LEU A 80 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 3 152.33 66.12
REMARK 500 1 SER A 8 -62.35 -144.52
REMARK 500 1 TRP A 9 157.04 65.80
REMARK 500 1 ASP A 20 111.99 -160.60
REMARK 500 1 ASP A 41 86.52 170.38
REMARK 500 1 LEU A 65 153.93 -47.93
REMARK 500 1 HIS A 71 90.12 -173.06
REMARK 500 1 CYS A 99 105.78 -56.54
REMARK 500 1 ARG A 104 86.67 -65.47
REMARK 500 1 HIS A 105 -26.39 160.33
REMARK 500 1 SER A 106 -65.06 84.84
REMARK 500 1 THR A 118 -84.12 -113.20
REMARK 500 1 LYS A 131 58.83 -90.14
REMARK 500 1 THR A 132 -38.79 -38.65
REMARK 500 1 SER A 133 85.87 55.03
REMARK 500 1 SER A 136 -57.91 74.73
REMARK 500 2 SER A 2 171.23 56.27
REMARK 500 2 SER A 3 150.01 62.37
REMARK 500 2 SER A 5 173.70 63.57
REMARK 500 2 SER A 6 148.01 66.01
REMARK 500 2 SER A 8 -54.42 -140.68
REMARK 500 2 TRP A 9 162.12 61.47
REMARK 500 2 ASN A 10 175.32 52.75
REMARK 500 2 THR A 31 -165.62 -79.09
REMARK 500 2 VAL A 36 79.78 -119.24
REMARK 500 2 SER A 38 153.28 -38.85
REMARK 500 2 HIS A 40 157.91 73.92
REMARK 500 2 HIS A 71 78.77 -161.83
REMARK 500 2 GLU A 75 34.61 -99.05
REMARK 500 2 ARG A 104 84.63 -59.23
REMARK 500 2 HIS A 105 177.39 171.79
REMARK 500 2 THR A 118 -84.89 -98.90
REMARK 500 2 SER A 119 -71.74 -38.95
REMARK 500 2 SER A 133 81.82 43.32
REMARK 500 3 SER A 2 175.88 179.14
REMARK 500 3 SER A 3 -63.12 69.47
REMARK 500 3 SER A 5 170.24 177.94
REMARK 500 3 SER A 6 168.73 178.19
REMARK 500 3 TRP A 9 64.86 80.36
REMARK 500 3 ASN A 10 163.94 177.93
REMARK 500 3 GLN A 11 162.94 -46.15
REMARK 500 3 SER A 38 95.75 -169.75
REMARK 500 3 HIS A 40 159.96 -49.08
REMARK 500 3 ASP A 41 154.51 72.14
REMARK 500 3 CYS A 44 179.42 72.89
REMARK 500 3 HIS A 71 77.25 -160.34
REMARK 500 3 VAL A 79 119.75 -166.99
REMARK 500 3 CYS A 99 150.37 -46.98
REMARK 500 3 ARG A 101 -67.07 -171.84
REMARK 500 3 SER A 103 36.92 84.07
REMARK 500
REMARK 500 THIS ENTRY HAS 324 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001399.1 RELATED DB: TARGETDB
DBREF 1WFM A 8 132 UNP Q7L8C5 SYT13_HUMAN 155 279
SEQADV 1WFM GLY A 1 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM SER A 2 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM SER A 3 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM GLY A 4 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM SER A 5 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM SER A 6 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM GLY A 7 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM SER A 133 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM GLY A 134 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM PRO A 135 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM SER A 136 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM SER A 137 UNP Q7L8C5 CLONING ARTIFACT
SEQADV 1WFM GLY A 138 UNP Q7L8C5 CLONING ARTIFACT
SEQRES 1 A 138 GLY SER SER GLY SER SER GLY SER TRP ASN GLN ALA PRO
SEQRES 2 A 138 LYS LEU HIS TYR CYS LEU ASP TYR ASP CYS GLN LYS ALA
SEQRES 3 A 138 GLU LEU PHE VAL THR ARG LEU GLU ALA VAL THR SER ASN
SEQRES 4 A 138 HIS ASP GLY GLY CYS ASP CYS TYR VAL GLN GLY SER VAL
SEQRES 5 A 138 ALA ASN ARG THR GLY SER VAL GLU ALA GLN THR ALA LEU
SEQRES 6 A 138 LYS LYS ARG GLN LEU HIS THR THR TRP GLU GLU GLY LEU
SEQRES 7 A 138 VAL LEU PRO LEU ALA GLU GLU GLU LEU PRO THR ALA THR
SEQRES 8 A 138 LEU THR LEU THR LEU ARG THR CYS ASP ARG PHE SER ARG
SEQRES 9 A 138 HIS SER VAL ALA GLY GLU LEU ARG LEU GLY LEU ASP GLY
SEQRES 10 A 138 THR SER VAL PRO LEU GLY ALA ALA GLN TRP GLY GLU LEU
SEQRES 11 A 138 LYS THR SER GLY PRO SER SER GLY
SHEET 1 A 3 THR A 72 THR A 73 0
SHEET 2 A 3 GLU A 27 VAL A 36 -1 N ALA A 35 O THR A 72
SHEET 3 A 3 LEU A 78 PRO A 81 -1 O LEU A 80 N LEU A 28
SHEET 1 B 4 THR A 72 THR A 73 0
SHEET 2 B 4 GLU A 27 VAL A 36 -1 N ALA A 35 O THR A 72
SHEET 3 B 4 LYS A 14 TYR A 21 -1 N LYS A 14 O VAL A 36
SHEET 4 B 4 GLN A 126 GLU A 129 -1 O GLY A 128 N LEU A 15
SHEET 1 C 4 GLY A 57 GLN A 62 0
SHEET 2 C 4 CYS A 46 ASN A 54 -1 N VAL A 52 O VAL A 59
SHEET 3 C 4 THR A 91 THR A 98 -1 O THR A 93 N SER A 51
SHEET 4 C 4 GLY A 109 GLY A 114 -1 O LEU A 111 N LEU A 94
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