Header list of 1sj6.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 03-MAR-04 1SJ6
TITLE NMR STRUCTURE AND REGULATED EXPRESSION IN APL CELL OF HUMAN SH3BGRL3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SH3 DOMAIN-BINDING GLUTAMIC ACID-RICH-LIKE PROTEIN 3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SH3 DOMAIN-BINDING PROTEIN SH3BP-1, P1725, TNF INHIBITORY
COMPND 5 PROTEIN, SH3BGRL3-LIKE PROTEIN;
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: SHEBGRL3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS THIOREDOXIN, NUCLEAR PROTEIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.XU,Y.TANG,Y.XU,J.WU,Y.SHI,Q.ZHANG,P.ZHENG,Y.DU
REVDAT 4 02-MAR-22 1SJ6 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1SJ6 1 VERSN
REVDAT 2 31-MAY-05 1SJ6 1 JRNL
REVDAT 1 22-MAR-05 1SJ6 0
JRNL AUTH C.XU,P.ZHENG,S.SHEN,Y.XU,L.WEI,H.GAO,S.WANG,C.ZHU,Y.TANG,
JRNL AUTH 2 J.WU,Q.ZHANG,Y.SHI
JRNL TITL NMR STRUCTURE AND REGULATED EXPRESSION IN APL CELL OF HUMAN
JRNL TITL 2 SH3BGRL3.
JRNL REF FEBS LETT. V. 579 2788 2005
JRNL REFN ISSN 0014-5793
JRNL PMID 15907482
JRNL DOI 10.1016/J.FEBSLET.2005.04.011
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, CNS 1.1
REMARK 3 AUTHORS : F.DELAGLIO (NMRPIPE), A.T.BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1463 RESTRAINTS, 1306 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 101
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 56 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS
REMARK 4
REMARK 4 1SJ6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021751.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM NACL, 20MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM SH3BGRL3 U-15N, 13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL,
REMARK 210 PH7.0; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D HCCH-COSY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 3D CBCA(CO)NH;
REMARK 210 3D_CBCANH; 3D HNCO; 3D_H(CCO)NH_
REMARK 210 TOCSY; 3D_C(CO)NH_TOCSY; 3D HCCH-
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, SPARKY SPARKY3
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 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 LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 96
REMARK 465 HIS A 97
REMARK 465 HIS A 98
REMARK 465 HIS A 99
REMARK 465 HIS A 100
REMARK 465 HIS A 101
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 GLN A 87 H LEU A 92 1.59
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 THR A 12 144.68 63.38
REMARK 500 1 ASN A 56 113.58 179.49
REMARK 500 1 ALA A 59 -166.16 -57.29
REMARK 500 1 ASN A 66 78.92 -109.55
REMARK 500 1 ASP A 68 37.06 -148.02
REMARK 500 1 LEU A 90 -67.62 -96.35
REMARK 500 1 ALA A 93 68.81 61.40
REMARK 500 1 LEU A 94 30.32 -98.29
REMARK 500 2 VAL A 11 73.83 -102.43
REMARK 500 2 GLN A 34 54.09 -98.66
REMARK 500 2 ASN A 56 114.70 176.56
REMARK 500 2 ALA A 59 -162.80 -58.42
REMARK 500 2 ASP A 68 28.54 -161.24
REMARK 500 2 LEU A 90 -65.44 -100.10
REMARK 500 2 LEU A 92 27.63 48.34
REMARK 500 3 ASN A 56 113.44 179.33
REMARK 500 3 ALA A 59 -165.41 -60.67
REMARK 500 3 PRO A 62 86.82 -67.35
REMARK 500 3 ASN A 66 78.90 -105.64
REMARK 500 3 ASP A 68 41.05 -145.28
REMARK 500 3 ASP A 73 -164.50 -160.04
REMARK 500 3 LEU A 86 -42.85 -29.10
REMARK 500 3 LEU A 90 -71.71 -95.11
REMARK 500 3 LEU A 92 -80.35 58.73
REMARK 500 3 ALA A 93 -42.59 -168.39
REMARK 500 3 LEU A 94 104.01 62.16
REMARK 500 4 GLN A 42 -57.08 -163.52
REMARK 500 4 ASN A 56 115.83 -179.77
REMARK 500 4 ALA A 59 -166.01 -57.73
REMARK 500 4 ASN A 66 43.08 -97.56
REMARK 500 4 LEU A 90 -67.20 -100.16
REMARK 500 4 LEU A 92 25.85 49.81
REMARK 500 5 SER A 14 -167.13 -75.58
REMARK 500 5 ARG A 32 41.95 70.81
REMARK 500 5 GLN A 34 51.47 -112.36
REMARK 500 5 ASN A 56 113.54 178.52
REMARK 500 5 ALA A 59 -165.21 -57.95
REMARK 500 5 ASP A 68 30.12 -161.81
REMARK 500 5 ASP A 73 -165.09 -160.11
REMARK 500 5 LEU A 90 -72.11 -98.78
REMARK 500 5 LEU A 92 -74.45 61.65
REMARK 500 5 ALA A 93 -68.86 -148.17
REMARK 500 6 GLN A 34 54.11 -98.89
REMARK 500 6 ASN A 56 113.28 -179.83
REMARK 500 6 ALA A 59 -165.74 -58.91
REMARK 500 6 PRO A 62 95.82 -60.56
REMARK 500 6 ASP A 68 35.10 70.81
REMARK 500 6 LEU A 90 -66.50 -100.10
REMARK 500 6 LEU A 92 27.98 47.59
REMARK 500 6 ALA A 93 33.69 -97.53
REMARK 500
REMARK 500 THIS ENTRY HAS 185 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SJ6 A 1 93 UNP Q9H299 SH3L3_HUMAN 1 93
SEQADV 1SJ6 LEU A 94 UNP Q9H299 EXPRESSION TAG
SEQADV 1SJ6 GLU A 95 UNP Q9H299 EXPRESSION TAG
SEQADV 1SJ6 HIS A 96 UNP Q9H299 EXPRESSION TAG
SEQADV 1SJ6 HIS A 97 UNP Q9H299 EXPRESSION TAG
SEQADV 1SJ6 HIS A 98 UNP Q9H299 EXPRESSION TAG
SEQADV 1SJ6 HIS A 99 UNP Q9H299 EXPRESSION TAG
SEQADV 1SJ6 HIS A 100 UNP Q9H299 EXPRESSION TAG
SEQADV 1SJ6 HIS A 101 UNP Q9H299 EXPRESSION TAG
SEQRES 1 A 101 MET SER GLY LEU ARG VAL TYR SER THR SER VAL THR GLY
SEQRES 2 A 101 SER ARG GLU ILE LYS SER GLN GLN SER GLU VAL THR ARG
SEQRES 3 A 101 ILE LEU ASP GLY LYS ARG ILE GLN TYR GLN LEU VAL ASP
SEQRES 4 A 101 ILE SER GLN ASP ASN ALA LEU ARG ASP GLU MET ARG ALA
SEQRES 5 A 101 LEU ALA GLY ASN PRO LYS ALA THR PRO PRO GLN ILE VAL
SEQRES 6 A 101 ASN GLY ASP GLN TYR CYS GLY ASP TYR GLU LEU PHE VAL
SEQRES 7 A 101 GLU ALA VAL GLU GLN ASN THR LEU GLN GLU PHE LEU LYS
SEQRES 8 A 101 LEU ALA LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 GLU A 16 LYS A 31 1 16
HELIX 2 2 ASP A 43 ALA A 54 1 12
HELIX 3 3 TYR A 74 GLU A 82 1 9
HELIX 4 4 THR A 85 LYS A 91 1 7
SHEET 1 A 4 GLN A 36 ASP A 39 0
SHEET 2 A 4 ARG A 5 SER A 8 1 N VAL A 6 O VAL A 38
SHEET 3 A 4 GLN A 63 VAL A 65 -1 O VAL A 65 N ARG A 5
SHEET 4 A 4 TYR A 70 ASP A 73 -1 O GLY A 72 N ILE A 64
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