Header list of 1wf2.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 25-MAY-04 1WF2
TITLE SOLUTION STRUCTURE OF RRM DOMAIN IN HNRPC PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS C1/C2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RRM DOMAIN;
COMPND 5 SYNONYM: HNRPC PROTEIN, HNRNP C1 / HNRNP C2;
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: ADKA0528;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040301-06;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURAL GENOMICS, RRM DOMAIN, HNRPC PROTEIN, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.HE,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WF2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WF2 1 VERSN
REVDAT 1 25-NOV-04 1WF2 0
JRNL AUTH F.HE,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RRM DOMAIN IN HNRPC PROTEIN
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 2.0.29
REMARK 3 AUTHORS : RUKER (XWINNMR), GUENTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WF2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000023508.
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 : 0.8MM U-15,13C; 20MM D-TRIS
REMARK 210 -HCL(PH 7.0); 100MM NACL; 1MM D-
REMARK 210 DTT; 0.02% NAN3; 90% H2O, 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 0.863, CYANA 2.0.29
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 HIS A 49 H PHE A 52 1.52
REMARK 500 O SER A 47 H PHE A 54 1.56
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 5 82.71 62.87
REMARK 500 1 ARG A 12 -57.80 -129.90
REMARK 500 1 SER A 13 75.92 -170.43
REMARK 500 1 ASN A 15 -46.51 -152.81
REMARK 500 1 ASN A 24 65.50 -69.59
REMARK 500 1 VAL A 27 -48.82 -132.97
REMARK 500 1 LYS A 50 99.06 -40.20
REMARK 500 1 ASP A 71 112.17 -39.69
REMARK 500 1 ALA A 85 76.97 -67.31
REMARK 500 1 ALA A 86 -53.33 -165.83
REMARK 500 1 ASN A 91 98.66 52.81
REMARK 500 2 SER A 2 80.21 55.87
REMARK 500 2 SER A 5 83.15 57.38
REMARK 500 2 ARG A 12 158.44 177.21
REMARK 500 2 MET A 14 82.89 38.20
REMARK 500 2 ASN A 24 66.98 -68.80
REMARK 500 2 VAL A 27 -51.13 -134.92
REMARK 500 2 LYS A 50 98.12 -40.07
REMARK 500 2 ASP A 71 113.42 -39.88
REMARK 500 2 ALA A 85 73.38 -68.13
REMARK 500 2 ALA A 86 -49.76 -165.04
REMARK 500 2 ARG A 92 -54.72 -151.56
REMARK 500 2 SER A 93 -58.53 177.16
REMARK 500 3 SER A 3 165.63 61.00
REMARK 500 3 SER A 5 -71.38 67.13
REMARK 500 3 THR A 9 117.36 60.38
REMARK 500 3 ARG A 12 100.23 52.12
REMARK 500 3 VAL A 27 -47.72 -134.89
REMARK 500 3 LYS A 50 96.10 -45.80
REMARK 500 3 PHE A 52 -166.16 -162.19
REMARK 500 3 GLU A 70 -70.99 -38.60
REMARK 500 3 ASP A 71 118.44 -37.92
REMARK 500 3 ALA A 76 -2.25 81.96
REMARK 500 3 ALA A 85 74.61 -68.50
REMARK 500 3 ALA A 86 -52.52 -160.79
REMARK 500 3 SER A 97 89.66 -156.71
REMARK 500 4 SER A 3 161.20 -43.62
REMARK 500 4 SER A 5 151.18 63.55
REMARK 500 4 SER A 6 -56.02 -144.77
REMARK 500 4 ARG A 12 134.03 -171.77
REMARK 500 4 SER A 13 -54.69 -140.21
REMARK 500 4 MET A 14 80.86 -151.87
REMARK 500 4 VAL A 27 -47.67 -135.43
REMARK 500 4 LYS A 50 97.91 -40.22
REMARK 500 4 ASP A 71 109.52 -38.76
REMARK 500 4 ALA A 76 -6.41 83.67
REMARK 500 4 ALA A 85 82.28 -64.69
REMARK 500 4 ALA A 86 -64.49 -171.54
REMARK 500 4 ASN A 91 94.29 49.27
REMARK 500 4 ARG A 92 144.01 -175.65
REMARK 500
REMARK 500 THIS ENTRY HAS 275 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000057.1 RELATED DB: TARGETDB
DBREF 1WF2 A 8 92 UNP P07910 HNRPC_HUMAN 8 92
SEQADV 1WF2 GLY A 1 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 SER A 2 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 SER A 3 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 GLY A 4 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 SER A 5 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 SER A 6 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 GLY A 7 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 SER A 93 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 GLY A 94 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 PRO A 95 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 SER A 96 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 SER A 97 UNP P07910 CLONING ARTIFACT
SEQADV 1WF2 GLY A 98 UNP P07910 CLONING ARTIFACT
SEQRES 1 A 98 GLY SER SER GLY SER SER GLY LYS THR ASP PRO ARG SER
SEQRES 2 A 98 MET ASN SER ARG VAL PHE ILE GLY ASN LEU ASN THR LEU
SEQRES 3 A 98 VAL VAL LYS LYS SER ASP VAL GLU ALA ILE PHE SER LYS
SEQRES 4 A 98 TYR GLY LYS ILE VAL GLY CYS SER VAL HIS LYS GLY PHE
SEQRES 5 A 98 ALA PHE VAL GLN TYR VAL ASN GLU ARG ASN ALA ARG ALA
SEQRES 6 A 98 ALA VAL ALA GLY GLU ASP GLY ARG MET ILE ALA GLY GLN
SEQRES 7 A 98 VAL LEU ASP ILE ASN LEU ALA ALA GLU PRO LYS VAL ASN
SEQRES 8 A 98 ARG SER GLY PRO SER SER GLY
HELIX 1 1 LYS A 30 PHE A 37 1 8
HELIX 2 2 SER A 38 TYR A 40 5 3
HELIX 3 3 GLU A 60 GLY A 69 1 10
SHEET 1 A 6 VAL A 18 GLY A 21 0
SHEET 2 A 6 ILE A 43 HIS A 49 1
SHEET 3 A 6 PHE A 52 TYR A 57 1
SHEET 4 A 6 MET A 74 ILE A 75 -1
SHEET 5 A 6 GLN A 78 VAL A 79 -1
SHEET 6 A 6 ASP A 81 LEU A 84 -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