Header list of 1wgv.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAY-04 1WGV
TITLE SOLUTION STRUCTURE OF THE CS DOMAIN OF HUMAN KIAA1068 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA1068 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CS 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 HJ05437;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040114-35;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CS DOMAIN, HSP20-LIKE FOLD, KIAA1068 PROTEIN, STRUCTURAL GENOMICS,
KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,F.HAYASHI,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WGV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WGV 1 VERSN
REVDAT 1 28-NOV-04 1WGV 0
JRNL AUTH H.LI,F.HAYASHI,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CS DOMAIN OF HUMAN KIAA1068
JRNL TITL 2 PROTEIN
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 1WGV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023565.
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 : 1.06MM CS DOMAIN OF HUMAN
REMARK 210 KIAA1068 PROTEIN U-13C, 15N;
REMARK 210 20MM D-TRIS-HCL (PH7.0); 100MM
REMARK 210 NACL; 2MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O
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 0.897, 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 OE2 GLU A 32 HH21 ARG A 34 1.54
REMARK 500 O VAL A 35 H VAL A 93 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 ASP A 12 -52.18 -149.62
REMARK 500 1 TYR A 14 91.23 -57.73
REMARK 500 1 ASN A 15 113.42 59.96
REMARK 500 1 ASN A 21 -58.72 -168.81
REMARK 500 1 TYR A 28 -75.72 -38.47
REMARK 500 1 ASP A 30 147.21 166.37
REMARK 500 1 SER A 52 -64.82 -127.34
REMARK 500 1 SER A 53 -54.77 178.31
REMARK 500 1 GLU A 62 -67.46 -93.54
REMARK 500 1 GLU A 63 -65.00 -166.42
REMARK 500 1 ASN A 79 75.87 -113.64
REMARK 500 1 LYS A 91 -100.27 -148.85
REMARK 500 1 VAL A 100 41.47 -97.68
REMARK 500 1 ILE A 115 164.65 -47.24
REMARK 500 1 SER A 122 -55.06 -135.37
REMARK 500 2 SER A 2 166.01 63.26
REMARK 500 2 SER A 3 83.29 44.23
REMARK 500 2 SER A 5 86.35 47.41
REMARK 500 2 ASP A 12 -64.29 76.53
REMARK 500 2 SER A 13 -62.60 -128.53
REMARK 500 2 ASN A 15 95.61 -57.00
REMARK 500 2 ASN A 21 -60.42 -172.26
REMARK 500 2 ASP A 30 144.44 166.47
REMARK 500 2 SER A 54 53.62 -148.86
REMARK 500 2 SER A 55 134.66 173.49
REMARK 500 2 GLU A 62 -84.86 -102.87
REMARK 500 2 GLU A 63 -45.97 -165.13
REMARK 500 2 LYS A 91 -102.75 -146.22
REMARK 500 2 GLU A 102 93.63 -67.13
REMARK 500 2 TRP A 105 -71.24 -102.01
REMARK 500 2 ASN A 106 -52.67 80.20
REMARK 500 2 SER A 122 132.10 -175.25
REMARK 500 3 SER A 2 85.37 -176.79
REMARK 500 3 SER A 3 96.26 66.78
REMARK 500 3 SER A 5 116.47 -163.04
REMARK 500 3 SER A 6 -59.14 -175.26
REMARK 500 3 GLN A 8 164.59 61.04
REMARK 500 3 ASN A 15 103.03 -170.29
REMARK 500 3 ALA A 17 122.31 -176.88
REMARK 500 3 ARG A 19 157.70 173.72
REMARK 500 3 ASN A 21 -62.65 173.54
REMARK 500 3 ASP A 30 153.50 172.41
REMARK 500 3 SER A 52 -65.55 -123.36
REMARK 500 3 SER A 53 -55.51 178.39
REMARK 500 3 ASN A 64 49.88 -150.86
REMARK 500 3 ASN A 79 76.61 -117.32
REMARK 500 3 LYS A 91 -97.71 -157.46
REMARK 500 3 VAL A 100 44.87 -102.68
REMARK 500 3 ALA A 107 133.02 -178.28
REMARK 500 3 GLU A 113 164.83 -44.88
REMARK 500
REMARK 500 THIS ENTRY HAS 415 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001044.1 RELATED DB: TARGETDB
DBREF 1WGV A 8 118 UNP Q8IVD9 NUDC3_HUMAN 169 279
SEQADV 1WGV GLY A 1 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV SER A 2 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV SER A 3 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV GLY A 4 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV SER A 5 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV SER A 6 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV GLY A 7 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV SER A 119 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV GLY A 120 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV PRO A 121 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV SER A 122 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV SER A 123 UNP Q8IVD9 CLONING ARTIFACT
SEQADV 1WGV GLY A 124 UNP Q8IVD9 CLONING ARTIFACT
SEQRES 1 A 124 GLY SER SER GLY SER SER GLY GLN LYS ASN PRO ASP SER
SEQRES 2 A 124 TYR ASN GLY ALA VAL ARG GLU ASN TYR THR TRP SER GLN
SEQRES 3 A 124 ASP TYR THR ASP LEU GLU VAL ARG VAL PRO VAL PRO LYS
SEQRES 4 A 124 HIS VAL VAL LYS GLY LYS GLN VAL SER VAL ALA LEU SER
SEQRES 5 A 124 SER SER SER ILE ARG VAL ALA MET LEU GLU GLU ASN GLY
SEQRES 6 A 124 GLU ARG VAL LEU MET GLU GLY LYS LEU THR HIS LYS ILE
SEQRES 7 A 124 ASN THR GLU SER SER LEU TRP SER LEU GLU PRO GLY LYS
SEQRES 8 A 124 CYS VAL LEU VAL ASN LEU SER LYS VAL GLY GLU TYR TRP
SEQRES 9 A 124 TRP ASN ALA ILE LEU GLU GLY GLU GLU PRO ILE ASP ILE
SEQRES 10 A 124 ASP SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 44 GLN A 46 5 3
SHEET 1 A 4 THR A 23 ASP A 27 0
SHEET 2 A 4 ASP A 30 PRO A 36 -1 O ARG A 34 N THR A 23
SHEET 3 A 4 CYS A 92 LEU A 97 -1 O VAL A 93 N VAL A 35
SHEET 4 A 4 LEU A 84 LEU A 87 -1 N SER A 86 O LEU A 94
SHEET 1 B 3 VAL A 47 SER A 52 0
SHEET 2 B 3 SER A 55 LEU A 61 -1 O ALA A 59 N SER A 48
SHEET 3 B 3 GLU A 66 LYS A 73 -1 O ARG A 67 N MET A 60
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