Header list of 1v5j.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 25-NOV-03 1V5J
TITLE SOLUTION STRUCTURE OF RSGI RUH-008, FN3 DOMAIN IN HUMAN CDNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA1355 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FN3 DOMAIN;
COMPND 5 SYNONYM: RSGI RUH-008;
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 KIAA1355;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021007-47;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS FN3 DOMAIN, HUMAN CDNA, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.DOI-KATAYAMA,F.HAYASHI,H.HIROTA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V5J 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V5J 1 VERSN
REVDAT 1 25-MAY-04 1V5J 0
JRNL AUTH Y.DOI-KATAYAMA,F.HAYASHI,H.HIROTA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RSGI RUH-008, A FN3 DOMAIN IN HUMAN
JRNL TITL 2 CDNA
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 1V5J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000006232.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3MM FN3 DOMAIN U-15, 13C; 20MM
REMARK 210 SODIUM PHOSPHATE; 100MM NACL;
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 : 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 0.822, 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, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, 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 ARG A 45 H GLU A 77 1.49
REMARK 500 H VAL A 17 O LEU A 24 1.53
REMARK 500 H THR A 19 O GLY A 22 1.60
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 87.20 43.83
REMARK 500 1 SER A 5 103.87 -160.86
REMARK 500 1 LYS A 35 -89.31 177.94
REMARK 500 1 ARG A 45 154.50 177.44
REMARK 500 1 TRP A 51 105.06 -57.99
REMARK 500 1 ASP A 55 103.33 -165.75
REMARK 500 1 ALA A 59 131.22 -37.22
REMARK 500 1 SER A 92 165.52 -41.22
REMARK 500 1 ASN A 93 154.61 -37.08
REMARK 500 1 THR A 99 63.90 -157.65
REMARK 500 1 SER A 103 72.12 44.67
REMARK 500 1 SER A 106 137.99 -175.34
REMARK 500 2 SER A 3 33.76 -92.88
REMARK 500 2 LYS A 35 -88.17 174.20
REMARK 500 2 ARG A 45 153.81 176.16
REMARK 500 2 VAL A 53 104.19 -46.01
REMARK 500 2 ALA A 59 131.32 -36.63
REMARK 500 2 LEU A 70 174.48 -47.95
REMARK 500 2 ASP A 73 19.58 54.74
REMARK 500 2 SER A 86 -58.47 90.94
REMARK 500 2 SER A 92 169.69 -43.28
REMARK 500 2 ASN A 93 160.17 -39.16
REMARK 500 2 THR A 99 73.83 -160.24
REMARK 500 2 SER A 107 126.48 -176.92
REMARK 500 3 SER A 2 -57.16 -138.19
REMARK 500 3 SER A 5 135.73 68.96
REMARK 500 3 SER A 6 -81.88 177.14
REMARK 500 3 LYS A 35 -106.09 -148.54
REMARK 500 3 ARG A 45 150.18 177.48
REMARK 500 3 SER A 48 -56.63 78.98
REMARK 500 3 GLN A 49 -144.69 25.36
REMARK 500 3 TRP A 51 105.16 -41.13
REMARK 500 3 ALA A 59 125.31 -37.96
REMARK 500 3 SER A 86 -60.36 87.76
REMARK 500 3 SER A 92 173.30 -45.51
REMARK 500 3 ASN A 93 168.14 -43.50
REMARK 500 3 SER A 103 -67.95 67.86
REMARK 500 4 SER A 5 74.60 -104.15
REMARK 500 4 LYS A 35 -90.25 172.30
REMARK 500 4 ARG A 45 153.20 176.49
REMARK 500 4 SER A 48 50.91 -118.66
REMARK 500 4 ALA A 59 128.35 -36.56
REMARK 500 4 SER A 92 172.57 -45.54
REMARK 500 4 ASN A 93 158.80 -39.68
REMARK 500 4 THR A 99 31.37 -157.74
REMARK 500 4 SER A 103 -63.32 80.40
REMARK 500 5 SER A 3 34.95 -91.27
REMARK 500 5 LEU A 14 98.30 -56.99
REMARK 500 5 LYS A 35 -86.36 177.22
REMARK 500 5 ARG A 45 147.38 178.15
REMARK 500
REMARK 500 THIS ENTRY HAS 228 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: HSK002001328.1 RELATED DB: TARGETDB
DBREF 1V5J A 8 102 GB 7243091 BAA92593 634 728
SEQADV 1V5J GLY A 1 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J SER A 2 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J SER A 3 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J GLY A 4 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J SER A 5 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J SER A 6 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J GLY A 7 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J SER A 103 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J GLY A 104 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J PRO A 105 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J SER A 106 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J SER A 107 GB 7243091 CLONING ARTIFACT
SEQADV 1V5J GLY A 108 GB 7243091 CLONING ARTIFACT
SEQRES 1 A 108 GLY SER SER GLY SER SER GLY LEU SER PRO PRO ARG GLY
SEQRES 2 A 108 LEU VAL ALA VAL ARG THR PRO ARG GLY VAL LEU LEU HIS
SEQRES 3 A 108 TRP ASP PRO PRO GLU LEU VAL PRO LYS ARG LEU ASP GLY
SEQRES 4 A 108 TYR VAL LEU GLU GLY ARG GLN GLY SER GLN GLY TRP GLU
SEQRES 5 A 108 VAL LEU ASP PRO ALA VAL ALA GLY THR GLU THR GLU LEU
SEQRES 6 A 108 LEU VAL PRO GLY LEU ILE LYS ASP VAL LEU TYR GLU PHE
SEQRES 7 A 108 ARG LEU VAL ALA PHE ALA GLY SER PHE VAL SER ASP PRO
SEQRES 8 A 108 SER ASN THR ALA ASN VAL SER THR SER GLY LEU SER GLY
SEQRES 9 A 108 PRO SER SER GLY
SHEET 1 A 6 ARG A 12 THR A 19 0
SHEET 2 A 6 GLY A 22 ASP A 28 -1
SHEET 3 A 6 TYR A 40 GLN A 46 -1
SHEET 4 A 6 GLU A 52 VAL A 58 -1
SHEET 5 A 6 GLU A 64 VAL A 67 -1
SHEET 6 A 6 PHE A 87 ASN A 96 -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