Header list of 1x4b.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 14-MAY-05 1X4B
TITLE SOLUTION STRUCTURE OF RRM DOMAIN IN HETEROGENEOUS NUCLEAR
TITLE 2 RIBONUCLEAOPROTEINS A2/B1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS A2/B1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RRM DOMAIN;
COMPND 5 SYNONYM: HNRNP A2 / HNRNP B1;
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: HNRPA2B1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040510-06;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURE GENOMICS, RRM DOMAIN, HETEROGENEOUS NUCLEAR
KEYWDS 2 RIBONUCLEOPROTEINS A2/B1, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 4 STRUCTURAL 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 1X4B 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X4B 1 VERSN
REVDAT 1 14-NOV-05 1X4B 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 HETEROGENEOUS NUCLEAR
JRNL TITL 2 RIBONUCLEAOPROTEINS A2/B1
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 1X4B 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_1000024361.
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
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 3 161.87 178.29
REMARK 500 1 SER A 6 161.28 176.68
REMARK 500 1 MET A 8 97.52 -173.26
REMARK 500 1 LEU A 12 171.64 66.02
REMARK 500 1 THR A 14 103.98 56.19
REMARK 500 1 LYS A 20 -88.62 68.65
REMARK 500 1 LYS A 21 157.92 85.54
REMARK 500 1 ARG A 22 81.82 48.92
REMARK 500 1 SER A 36 -7.77 81.15
REMARK 500 1 PHE A 37 -2.17 75.22
REMARK 500 1 SER A 43 -37.35 -39.86
REMARK 500 1 ARG A 67 -77.32 -126.73
REMARK 500 1 ALA A 87 49.75 -98.76
REMARK 500 1 ALA A 88 52.29 -141.61
REMARK 500 1 ALA A 103 -49.70 84.83
REMARK 500 1 ALA A 105 90.47 42.19
REMARK 500 1 SER A 115 143.36 179.45
REMARK 500 2 SER A 6 157.63 178.06
REMARK 500 2 MET A 8 89.47 -174.66
REMARK 500 2 LEU A 17 109.00 -174.95
REMARK 500 2 GLU A 18 124.59 -178.50
REMARK 500 2 LYS A 20 -66.98 -139.91
REMARK 500 2 ARG A 22 140.30 174.19
REMARK 500 2 ARG A 28 44.10 -107.34
REMARK 500 2 SER A 36 -1.35 79.97
REMARK 500 2 PHE A 37 -2.35 75.70
REMARK 500 2 GLU A 38 -62.32 -105.10
REMARK 500 2 THR A 39 97.22 -39.05
REMARK 500 2 SER A 68 129.80 61.44
REMARK 500 2 ALA A 87 48.65 -101.18
REMARK 500 2 ALA A 103 55.30 -94.03
REMARK 500 2 ALA A 105 -74.61 73.47
REMARK 500 2 ARG A 106 150.71 -38.87
REMARK 500 2 GLU A 107 79.61 65.72
REMARK 500 2 SER A 109 105.51 57.57
REMARK 500 2 SER A 111 89.20 42.47
REMARK 500 2 SER A 114 148.82 -177.41
REMARK 500 2 SER A 115 96.18 178.40
REMARK 500 3 SER A 2 112.53 58.56
REMARK 500 3 GLU A 9 128.00 -175.81
REMARK 500 3 LYS A 10 -50.38 -176.50
REMARK 500 3 LEU A 12 79.96 -172.14
REMARK 500 3 LEU A 17 -64.48 -101.78
REMARK 500 3 GLU A 18 -69.58 -178.56
REMARK 500 3 ARG A 22 73.27 45.95
REMARK 500 3 GLU A 25 -65.02 -95.17
REMARK 500 3 PHE A 37 -2.33 75.67
REMARK 500 3 GLU A 38 -64.93 -106.12
REMARK 500 3 THR A 39 99.50 -37.66
REMARK 500 3 THR A 40 -164.79 -77.34
REMARK 500
REMARK 500 THIS ENTRY HAS 350 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: HSS001003384.2 RELATED DB: TARGETDB
DBREF 1X4B A 8 110 UNP P22626 ROA2_HUMAN 1 103
SEQADV 1X4B GLY A 1 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B SER A 2 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B SER A 3 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B GLY A 4 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B SER A 5 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B SER A 6 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B GLY A 7 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B SER A 111 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B GLY A 112 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B PRO A 113 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B SER A 114 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B SER A 115 UNP P22626 CLONING ARTIFACT
SEQADV 1X4B GLY A 116 UNP P22626 CLONING ARTIFACT
SEQRES 1 A 116 GLY SER SER GLY SER SER GLY MET GLU LYS THR LEU GLU
SEQRES 2 A 116 THR VAL PRO LEU GLU ARG LYS LYS ARG GLU LYS GLU GLN
SEQRES 3 A 116 PHE ARG LYS LEU PHE ILE GLY GLY LEU SER PHE GLU THR
SEQRES 4 A 116 THR GLU GLU SER LEU ARG ASN TYR TYR GLU GLN TRP GLY
SEQRES 5 A 116 LYS LEU THR ASP CYS VAL VAL MET ARG ASP PRO ALA SER
SEQRES 6 A 116 LYS ARG SER ARG GLY PHE GLY PHE VAL THR PHE SER SER
SEQRES 7 A 116 MET ALA GLU VAL ASP ALA ALA MET ALA ALA ARG PRO HIS
SEQRES 8 A 116 SER ILE ASP GLY ARG VAL VAL GLU PRO LYS ARG ALA VAL
SEQRES 9 A 116 ALA ARG GLU GLU SER GLY SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 23 PHE A 27 1 5
HELIX 2 2 GLU A 41 TYR A 48 1 8
HELIX 3 3 MET A 79 MET A 86 1 8
SHEET 1 A 5 LYS A 29 GLY A 33 0
SHEET 2 A 5 ASP A 56 MET A 60 0
SHEET 3 A 5 PHE A 71 THR A 75 -1
SHEET 4 A 5 HIS A 91 ILE A 93 0
SHEET 5 A 5 ARG A 96 LYS A 101 0
CISPEP 1 ARG A 89 PRO A 90 1 0.02
CISPEP 2 ARG A 89 PRO A 90 2 -0.03
CISPEP 3 ARG A 89 PRO A 90 3 0.04
CISPEP 4 ARG A 89 PRO A 90 4 -0.01
CISPEP 5 ARG A 89 PRO A 90 5 -0.05
CISPEP 6 ARG A 89 PRO A 90 6 0.03
CISPEP 7 ARG A 89 PRO A 90 7 0.01
CISPEP 8 ARG A 89 PRO A 90 8 0.03
CISPEP 9 ARG A 89 PRO A 90 9 -0.06
CISPEP 10 ARG A 89 PRO A 90 10 0.02
CISPEP 11 ARG A 89 PRO A 90 11 0.02
CISPEP 12 ARG A 89 PRO A 90 12 -0.04
CISPEP 13 ARG A 89 PRO A 90 13 0.05
CISPEP 14 ARG A 89 PRO A 90 14 -0.03
CISPEP 15 ARG A 89 PRO A 90 15 0.01
CISPEP 16 ARG A 89 PRO A 90 16 -0.01
CISPEP 17 ARG A 89 PRO A 90 17 0.02
CISPEP 18 ARG A 89 PRO A 90 18 0.01
CISPEP 19 ARG A 89 PRO A 90 19 0.03
CISPEP 20 ARG A 89 PRO A 90 20 0.05
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