Header list of 2crf.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSPORT PROTEIN 20-MAY-05 2CRF
TITLE SOLUTION STRUCTURE OF THE RAN_BP1 DOMAIN OF RAN-BINDING PROTEIN-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAN BINDING PROTEIN 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RAN_BP1 DOMAIN;
COMPND 5 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: RANBP3;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041004-03;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS RAN_BP1 DOMAIN, RAN-BINDING PROTEIN 3, RANBP3, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.P.ZHANG,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CRF 1 REMARK SEQADV SHEET
REVDAT 2 24-FEB-09 2CRF 1 VERSN
REVDAT 1 20-NOV-05 2CRF 0
JRNL AUTH H.P.ZHANG,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RAN_BP1 DOMAIN OF RAN-BINDING
JRNL TITL 2 PROTEIN-3
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 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CRF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024541.
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 : 1.37MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL (PH7.0); 200MM
REMARK 210 NACL; 1MM D-DTT; 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; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.04,
REMARK 210 KUJIRA 0.9296, CYANA 2.0.17
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, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: 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 3 118.24 -163.32
REMARK 500 1 THR A 8 109.30 -44.41
REMARK 500 1 ALA A 9 41.52 -84.64
REMARK 500 1 GLU A 23 33.45 35.04
REMARK 500 1 ALA A 25 39.26 36.40
REMARK 500 1 VAL A 29 -74.71 -55.16
REMARK 500 1 LYS A 41 -29.63 -37.69
REMARK 500 1 LEU A 67 99.38 -68.39
REMARK 500 1 SER A 78 39.69 -97.32
REMARK 500 1 LEU A 79 30.75 36.49
REMARK 500 1 LYS A 99 -31.46 -130.25
REMARK 500 1 ARG A 135 -31.34 -37.27
REMARK 500 2 GLU A 15 35.97 -83.79
REMARK 500 2 ALA A 25 41.29 -97.66
REMARK 500 2 VAL A 29 -70.61 -58.68
REMARK 500 2 LYS A 41 -27.15 -38.09
REMARK 500 2 LEU A 67 99.72 -68.87
REMARK 500 2 ASN A 84 105.69 -161.97
REMARK 500 2 GLN A 90 32.30 -84.05
REMARK 500 2 GLN A 111 35.99 39.41
REMARK 500 2 ALA A 131 -70.19 -64.88
REMARK 500 2 LEU A 132 -70.13 -37.91
REMARK 500 2 LEU A 137 -31.39 -37.70
REMARK 500 3 ALA A 9 145.34 -172.24
REMARK 500 3 CYS A 12 168.04 -47.79
REMARK 500 3 ALA A 25 43.94 -94.96
REMARK 500 3 LYS A 41 -35.16 -33.87
REMARK 500 3 GLN A 90 31.95 -84.37
REMARK 500 3 LEU A 128 -70.32 -50.58
REMARK 500 4 SER A 3 42.41 70.41
REMARK 500 4 CYS A 12 98.40 -39.15
REMARK 500 4 GLU A 15 73.12 -69.14
REMARK 500 4 GLU A 18 -36.70 -36.33
REMARK 500 4 THR A 21 153.51 -45.85
REMARK 500 4 ALA A 25 42.36 -83.14
REMARK 500 4 GLN A 44 43.03 36.86
REMARK 500 4 THR A 62 -60.62 -98.76
REMARK 500 4 GLN A 76 40.08 -81.84
REMARK 500 4 GLN A 90 31.51 -83.72
REMARK 500 4 GLN A 111 43.79 38.92
REMARK 500 4 SER A 122 -33.61 -36.30
REMARK 500 4 LEU A 132 -70.90 -53.76
REMARK 500 5 SER A 3 -49.01 -133.24
REMARK 500 5 GLU A 15 37.19 -91.82
REMARK 500 5 LYS A 41 -34.02 -33.21
REMARK 500 5 GLN A 44 48.38 38.03
REMARK 500 5 LEU A 79 75.71 -61.73
REMARK 500 5 GLN A 90 32.78 -82.87
REMARK 500 5 GLN A 111 49.00 38.87
REMARK 500 5 SER A 122 -31.94 -35.80
REMARK 500
REMARK 500 THIS ENTRY HAS 201 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: HSS001002253.1 RELATED DB: TARGETDB
DBREF 2CRF A 8 144 UNP Q9H6Z4 RANB3_HUMAN 375 511
SEQADV 2CRF GLY A 1 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF SER A 2 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF SER A 3 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF GLY A 4 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF SER A 5 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF SER A 6 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF GLY A 7 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF SER A 145 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF GLY A 146 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF PRO A 147 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF SER A 148 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF SER A 149 UNP Q9H6Z4 CLONING ARTIFACT
SEQADV 2CRF GLY A 150 UNP Q9H6Z4 CLONING ARTIFACT
SEQRES 1 A 150 GLY SER SER GLY SER SER GLY THR ALA ARG LYS CYS LEU
SEQRES 2 A 150 LEU GLU LYS VAL GLU VAL ILE THR GLY GLU GLU ALA GLU
SEQRES 3 A 150 SER ASN VAL LEU GLN MET GLN CYS LYS LEU PHE VAL PHE
SEQRES 4 A 150 ASP LYS THR SER GLN SER TRP VAL GLU ARG GLY ARG GLY
SEQRES 5 A 150 LEU LEU ARG LEU ASN ASP MET ALA SER THR ASP ASP GLY
SEQRES 6 A 150 THR LEU GLN SER ARG LEU VAL MET ARG THR GLN GLY SER
SEQRES 7 A 150 LEU ARG LEU ILE LEU ASN THR LYS LEU TRP ALA GLN MET
SEQRES 8 A 150 GLN ILE ASP LYS ALA SER GLU LYS SER ILE HIS ILE THR
SEQRES 9 A 150 ALA MET ASP THR GLU ASP GLN GLY VAL LYS VAL PHE LEU
SEQRES 10 A 150 ILE SER ALA SER SER LYS ASP THR GLY GLN LEU TYR ALA
SEQRES 11 A 150 ALA LEU HIS HIS ARG ILE LEU ALA LEU ARG SER ARG VAL
SEQRES 12 A 150 GLU SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 124 VAL A 143 1 20
SHEET 1 A 6 SER A 27 ASP A 40 0
SHEET 2 A 6 SER A 45 ALA A 60 -1
SHEET 3 A 6 LEU A 67 THR A 75 -1
SHEET 4 A 6 LEU A 81 LYS A 86 -1
SHEET 5 A 6 SER A 100 MET A 106 -1
SHEET 6 A 6 VAL A 113 SER A 119 -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 9 2 Bytes