Header list of 1x4a.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 14-MAY-05 1X4A
TITLE SOLUTION STRUCTURE OF RRM DOMAIN IN SPLICING FACTOR SF2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPLICING FACTOR, ARGININE/SERINE-RICH 1 (SPLICING FACTOR 2,
COMPND 3 ALTERNATE SPLICING FACTOR) VARIANT;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RRM DOMAIN;
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: SFRS1; ASF; SF2; SF2P33;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040315-67;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURE GENOMICS, SURP DOMAIN, SPLICING FACTOR SF2, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 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 1X4A 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X4A 1 VERSN
REVDAT 1 14-NOV-05 1X4A 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 SPLICING FACTOR SF2
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 1.0.8
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X4A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024360.
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 PHOSPHATE
REMARK 210 BUFFER NA; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3
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 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.863, CYANA 1.0.8
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 : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY
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 GLU A 75 H TYR A 79 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 3 162.38 179.35
REMARK 500 1 SER A 6 138.47 64.09
REMARK 500 1 SER A 9 160.73 179.46
REMARK 500 1 ASN A 20 113.05 -172.20
REMARK 500 1 ASP A 33 45.74 -102.84
REMARK 500 1 ASP A 51 144.84 -170.41
REMARK 500 1 LYS A 55 -75.12 -75.75
REMARK 500 1 ASN A 56 91.53 65.05
REMARK 500 1 ARG A 58 128.48 -39.89
REMARK 500 1 ASP A 82 93.87 -62.97
REMARK 500 1 SER A 98 -53.32 -159.00
REMARK 500 1 SER A 107 -57.98 -178.91
REMARK 500 1 SER A 108 92.30 62.17
REMARK 500 2 SER A 2 -58.47 -160.69
REMARK 500 2 ARG A 15 164.16 -47.77
REMARK 500 2 ASN A 21 173.13 53.66
REMARK 500 2 ASP A 33 50.12 -106.67
REMARK 500 2 LYS A 55 -79.64 -71.49
REMARK 500 2 ASN A 56 101.34 53.62
REMARK 500 2 ARG A 57 -46.77 179.54
REMARK 500 2 ARG A 81 -32.21 -38.86
REMARK 500 2 ASP A 82 99.86 -57.83
REMARK 500 2 ARG A 100 132.18 -174.21
REMARK 500 2 THR A 102 127.16 62.69
REMARK 500 2 SER A 104 161.94 67.24
REMARK 500 3 SER A 2 173.28 178.82
REMARK 500 3 SER A 3 158.70 62.36
REMARK 500 3 SER A 5 -60.76 -158.33
REMARK 500 3 SER A 6 167.60 57.25
REMARK 500 3 ALA A 18 168.01 55.64
REMARK 500 3 ASN A 29 17.21 59.08
REMARK 500 3 ASP A 33 50.71 -107.06
REMARK 500 3 TYR A 46 -60.14 -99.80
REMARK 500 3 ARG A 57 96.87 175.82
REMARK 500 3 ARG A 58 173.16 168.09
REMARK 500 3 ARG A 81 -37.72 -38.74
REMARK 500 3 ASP A 82 98.46 -43.41
REMARK 500 3 SER A 107 174.48 61.14
REMARK 500 4 SER A 2 124.79 -172.54
REMARK 500 4 MET A 8 -55.87 -121.08
REMARK 500 4 SER A 9 95.95 64.14
REMARK 500 4 VAL A 13 87.11 50.40
REMARK 500 4 ASN A 21 97.52 66.16
REMARK 500 4 ASP A 33 32.20 -99.14
REMARK 500 4 ASP A 51 144.90 178.35
REMARK 500 4 ASN A 56 88.60 49.56
REMARK 500 4 ARG A 57 -57.52 177.48
REMARK 500 4 ARG A 81 -38.70 -38.69
REMARK 500 4 ASP A 82 90.66 -54.15
REMARK 500 4 ARG A 97 170.56 62.13
REMARK 500
REMARK 500 THIS ENTRY HAS 269 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: HSS001003882 RELATED DB: TARGETDB
DBREF 1X4A A 8 103 UNP Q07955 SFRS1_HUMAN 33 128
SEQADV 1X4A GLY A 1 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A SER A 2 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A SER A 3 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A GLY A 4 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A SER A 5 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A SER A 6 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A GLY A 7 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A SER A 104 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A GLY A 105 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A PRO A 106 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A SER A 107 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A SER A 108 UNP Q07955 CLONING ARTIFACT
SEQADV 1X4A GLY A 109 UNP Q07955 CLONING ARTIFACT
SEQRES 1 A 109 GLY SER SER GLY SER SER GLY MET SER GLY GLY GLY VAL
SEQRES 2 A 109 ILE ARG GLY PRO ALA GLY ASN ASN ASP CYS ARG ILE TYR
SEQRES 3 A 109 VAL GLY ASN LEU PRO PRO ASP ILE ARG THR LYS ASP ILE
SEQRES 4 A 109 GLU ASP VAL PHE TYR LYS TYR GLY ALA ILE ARG ASP ILE
SEQRES 5 A 109 ASP LEU LYS ASN ARG ARG GLY GLY PRO PRO PHE ALA PHE
SEQRES 6 A 109 VAL GLU PHE GLU ASP PRO ARG ASP ALA GLU ASP ALA VAL
SEQRES 7 A 109 TYR GLY ARG ASP GLY TYR ASP TYR ASP GLY TYR ARG LEU
SEQRES 8 A 109 ARG VAL GLU PHE PRO ARG SER GLY ARG GLY THR GLY SER
SEQRES 9 A 109 GLY PRO SER SER GLY
HELIX 1 1 THR A 36 PHE A 43 1 8
HELIX 2 2 TYR A 44 TYR A 46 5 3
HELIX 3 3 PRO A 71 ARG A 81 1 11
SHEET 1 A 4 ARG A 24 GLY A 28 0
SHEET 2 A 4 ILE A 49 LEU A 54 -1
SHEET 3 A 4 ALA A 64 PHE A 68 -1
SHEET 4 A 4 ASP A 85 TYR A 86 -1
SHEET 1 B 2 TYR A 89 ARG A 90 0
SHEET 2 B 2 ARG A 92 GLU A 94 -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