Header list of 1ufw.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 10-JUN-03 1UFW
TITLE SOLUTION STRUCTURE OF RNP DOMAIN IN SYNAPTOJANIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPTOJANIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNP DOMAIN;
COMPND 5 EC: 3.1.3.36;
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 HG01551;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021015-22;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RNP DOMAIN, SYNAPTOJANIN 2, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.HE,Y.MUTO,R.USHIKOSHI,M.SHIROUZU,T.TERADA,T.KIGAWA,M.INOUE,
AUTHOR 2 T.YABUKI,M.AOKI,E.SEKI,T.MATSUDA,H.HIROTA,M.YOSHIDA,N.KOBAYASHI,
AUTHOR 3 A.TANAKA,T.OSANAI,Y.MATSUO,O.OHARA,T.NAGASE,R.KIKUNO,M.NAKAYAMA,
AUTHOR 4 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UFW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UFW 1 VERSN
REVDAT 1 10-DEC-03 1UFW 0
JRNL AUTH F.HE,Y.MUTO,R.USHIKOSHI,M.SHIROUZU,T.TERADA,T.KIGAWA,
JRNL AUTH 2 M.INOUE,T.YABUKI,M.AOKI,E.SEKI,T.MATSUDA,H.HIROTA,M.YOSHIDA,
JRNL AUTH 3 N.KOBAYASHI,A.TANAKA,T.OSANAI,Y.MATSUO,O.OHARA,T.NAGASE,
JRNL AUTH 4 R.KIKUNO,M.NAKAYAMA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RNP DOMAIN IN SYNAPTOJANIN 2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UFW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000005783.
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
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1MM RNP DOMAIN U-15N, 13C;
REMARK 210 20MM PHOSPHATE BUFFER NA(PH 6.0);
REMARK 210 100MM NACL; 0.02% NAN3; 90% H2O,
REMARK 210 10% D2O;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.811, 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 VAL A 77 H MET A 80 1.51
REMARK 500 O THR A 39 H GLN A 43 1.52
REMARK 500 O THR A 26 H LYS A 30 1.55
REMARK 500 O SER A 73 H VAL A 77 1.55
REMARK 500 O ARG A 38 H MET A 42 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 PHE A 10 94.74 45.92
REMARK 500 1 GLN A 11 107.82 -171.80
REMARK 500 1 ALA A 16 43.41 71.22
REMARK 500 1 GLU A 32 132.13 -174.32
REMARK 500 1 PHE A 33 132.50 -39.02
REMARK 500 1 ARG A 38 -75.22 -38.38
REMARK 500 1 MET A 61 89.94 -151.78
REMARK 500 1 MET A 80 169.93 -45.06
REMARK 500 1 SER A 94 116.42 -168.33
REMARK 500 2 SER A 8 87.05 62.39
REMARK 500 2 PHE A 10 100.56 50.13
REMARK 500 2 GLN A 11 -52.90 -140.43
REMARK 500 2 ALA A 16 36.41 81.68
REMARK 500 2 ARG A 38 -75.19 -39.21
REMARK 500 2 LEU A 53 149.07 174.26
REMARK 500 2 GLN A 58 -47.14 -26.07
REMARK 500 2 SER A 93 155.30 72.55
REMARK 500 3 SER A 2 75.25 -119.34
REMARK 500 3 SER A 3 -61.35 -96.41
REMARK 500 3 PHE A 10 175.18 51.95
REMARK 500 3 GLN A 11 86.51 59.50
REMARK 500 3 ALA A 16 38.72 80.85
REMARK 500 3 ARG A 38 -73.12 -41.18
REMARK 500 3 TYR A 48 -38.70 -37.77
REMARK 500 3 LEU A 53 148.32 173.48
REMARK 500 3 GLN A 60 -173.33 179.73
REMARK 500 3 MET A 61 103.34 -167.62
REMARK 500 3 SER A 94 86.00 67.14
REMARK 500 4 SER A 9 -62.13 -96.74
REMARK 500 4 PHE A 10 74.62 40.40
REMARK 500 4 GLN A 11 138.54 -173.80
REMARK 500 4 ALA A 16 37.76 79.59
REMARK 500 4 GLU A 32 139.75 -175.46
REMARK 500 4 ARG A 38 -75.45 -66.58
REMARK 500 4 THR A 44 -71.51 -67.19
REMARK 500 4 ILE A 51 94.20 -63.28
REMARK 500 4 GLN A 58 -51.38 -26.14
REMARK 500 4 MET A 80 173.18 -49.92
REMARK 500 4 PRO A 92 -165.69 -74.97
REMARK 500 4 SER A 94 162.69 56.99
REMARK 500 5 SER A 8 95.04 -169.78
REMARK 500 5 PHE A 10 -42.52 -168.15
REMARK 500 5 ALA A 16 57.27 71.26
REMARK 500 5 ARG A 38 -75.42 -37.31
REMARK 500 5 ILE A 51 97.22 -61.86
REMARK 500 5 LEU A 53 152.84 174.13
REMARK 500 5 GLN A 58 -51.98 -22.93
REMARK 500 5 MET A 80 160.04 -40.34
REMARK 500 6 SER A 2 -58.05 178.44
REMARK 500 6 SER A 8 115.96 -178.63
REMARK 500
REMARK 500 THIS ENTRY HAS 200 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000339.1 RELATED DB: TARGETDB
DBREF 1UFW A 8 89 UNP O15056 SYNJ2_HUMAN 829 910
SEQADV 1UFW GLY A 1 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW SER A 2 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW SER A 3 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW GLY A 4 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW SER A 5 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW SER A 6 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW GLY A 7 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW SER A 90 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW GLY A 91 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW PRO A 92 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW SER A 93 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW SER A 94 UNP O15056 CLONING ARTIFACT
SEQADV 1UFW GLY A 95 UNP O15056 CLONING ARTIFACT
SEQRES 1 A 95 GLY SER SER GLY SER SER GLY SER SER PHE GLN GLY PRO
SEQRES 2 A 95 LEU ASP ALA THR VAL VAL VAL ASN LEU GLN SER PRO THR
SEQRES 3 A 95 LEU GLU GLU LYS ASN GLU PHE PRO GLU ASP LEU ARG THR
SEQRES 4 A 95 GLU LEU MET GLN THR LEU GLY SER TYR GLY THR ILE VAL
SEQRES 5 A 95 LEU VAL ARG ILE ASN GLN GLY GLN MET LEU VAL THR PHE
SEQRES 6 A 95 ALA ASP SER HIS SER ALA LEU SER VAL LEU ASP VAL ASP
SEQRES 7 A 95 GLY MET LYS VAL LYS GLY ARG ALA VAL LYS ILE SER GLY
SEQRES 8 A 95 PRO SER SER GLY
HELIX 1 1 GLY A 4 GLY A 7 1 4
HELIX 2 2 LEU A 27 ASN A 31 1 5
HELIX 3 3 GLU A 35 TYR A 48 1 14
HELIX 4 4 HIS A 69 VAL A 77 1 9
SHEET 1 A 5 LEU A 53 ASN A 57 0
SHEET 2 A 5 GLN A 60 THR A 64 -1 O THR A 64 N LEU A 53
SHEET 3 A 5 THR A 17 LEU A 22 -1 N VAL A 18 O VAL A 63
SHEET 4 A 5 ARG A 85 SER A 90 -1 O LYS A 88 N ASN A 21
SHEET 5 A 5 LYS A 81 VAL A 82 -1 N VAL A 82 O ARG A 85
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