Header list of 1zzp.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 14-JUN-05 1ZZP
TITLE SOLUTION STRUCTURE OF THE F-ACTIN BINDING DOMAIN OF BCR-ABL/C-ABL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: F-ACTIN BINDING DOMAIN (RESIDUES 1007-1130);
COMPND 5 SYNONYM: P150, C-ABL;
COMPND 6 EC: 2.7.1.112;
COMPND 7 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: ABL1, ABL, JTK7;
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: MODIFIED PET24D
KEYWDS FOUR HELIX BUNDLE, NUCLEAR EXPORT SIGNAL, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR O.HANTSCHEL,S.WIESNER,T.GUTTLER,C.D.MACKERETH,L.L.R.RIX,Z.MIKES,
AUTHOR 2 J.DEHNE,D.GORLICH,M.SATTLER,G.SUPERTI-FURGA
REVDAT 3 09-MAR-22 1ZZP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZZP 1 VERSN
REVDAT 1 30-AUG-05 1ZZP 0
JRNL AUTH O.HANTSCHEL,S.WIESNER,T.GUTTLER,C.D.MACKERETH,L.L.R.RIX,
JRNL AUTH 2 Z.MIKES,J.DEHNE,D.GORLICH,M.SATTLER,G.SUPERTI-FURGA
JRNL TITL STRUCTURAL BASIS FOR THE CYTOSKELETAL ASSOCIATION OF
JRNL TITL 2 BCR-ABL/C-ABL.
JRNL REF MOL.CELL V. 19 461 2005
JRNL REFN ISSN 1097-2765
JRNL PMID 16109371
JRNL DOI 10.1016/J.MOLCEL.2005.06.030
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : NILGES, M.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZZP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033311.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295; 295
REMARK 210 PH : 6.3; 6.3
REMARK 210 IONIC STRENGTH : 20MM SODIUM PHOSPHATE, 150MM
REMARK 210 NACL, 0.02% (W/V) NAN3; 20MM
REMARK 210 SODIUM PHOSPHATE, 150MM NACL,
REMARK 210 0.02% (W/V) NAN3
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM U-15N,13C BCR-ABL/C-ABL
REMARK 210 FABD, 20MM PHOSPHATE BUFFER,
REMARK 210 100MM NACL, 0.02% NAN3, 5MM DTT,
REMARK 210 90% H2O, 10% D2O; 1MM U-15N,13C
REMARK 210 BCR-ABL/C-ABL FABD, 20MM
REMARK 210 PHOSPHATE BUFFER, 100MM NACL,
REMARK 210 0.02% NAN3, 5MM DTT, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, NMRPIPE, XEASY, NMRVIEW
REMARK 210 5.0.4
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 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 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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 10
REMARK 465 ALA A 11
REMARK 465 MET A 12
REMARK 465 ALA A 13
REMARK 465 SER A 14
REMARK 465 THR A 15
REMARK 465 ARG A 16
REMARK 465 VAL A 17
REMARK 465 SER A 18
REMARK 465 LEU A 19
REMARK 465 ARG A 20
REMARK 465 LYS A 21
REMARK 465 THR A 22
REMARK 465 ARG A 23
REMARK 465 GLN A 24
REMARK 465 PRO A 25
REMARK 465 PRO A 26
REMARK 465 GLU A 27
REMARK 465 ARG A 28
REMARK 465 ILE A 29
REMARK 465 ALA A 30
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 6 PHE A 121 CE1 PHE A 121 CZ 0.125
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 ILE A 34 98.65 64.76
REMARK 500 1 GLN A 56 41.19 -178.08
REMARK 500 1 MET A 57 -37.56 74.74
REMARK 500 1 ALA A 58 -117.08 50.45
REMARK 500 1 SER A 59 135.43 -174.47
REMARK 500 1 MET A 84 -91.05 81.91
REMARK 500 1 ARG A 85 0.92 -64.75
REMARK 500 1 GLN A 105 -95.44 -52.18
REMARK 500 1 ILE A 106 -48.84 -145.76
REMARK 500 1 CYS A 107 154.44 66.78
REMARK 500 1 ALA A 109 1.58 -166.79
REMARK 500 1 ALA A 111 -72.12 -68.25
REMARK 500 1 THR A 118 107.83 54.47
REMARK 500 1 PHE A 121 43.10 -85.02
REMARK 500 1 LEU A 138 -35.63 -132.16
REMARK 500 2 ALA A 33 18.78 -141.18
REMARK 500 2 ILE A 34 106.69 64.83
REMARK 500 2 THR A 35 -160.27 -123.45
REMARK 500 2 ALA A 58 -140.58 -102.23
REMARK 500 2 SER A 59 140.29 -175.73
REMARK 500 2 GLN A 82 -66.65 61.96
REMARK 500 2 GLN A 83 -9.33 -46.03
REMARK 500 2 MET A 84 -69.92 48.43
REMARK 500 2 GLN A 105 -177.87 -57.11
REMARK 500 2 CYS A 107 95.72 25.64
REMARK 500 2 ALA A 109 9.11 -174.08
REMARK 500 2 ALA A 116 84.37 53.61
REMARK 500 2 THR A 118 77.78 47.79
REMARK 500 2 PHE A 121 42.83 -78.46
REMARK 500 2 LEU A 138 -74.57 -62.71
REMARK 500 3 ALA A 33 21.82 49.79
REMARK 500 3 ILE A 34 107.77 62.66
REMARK 500 3 THR A 35 -160.35 -124.02
REMARK 500 3 GLN A 56 -139.56 -172.49
REMARK 500 3 ALA A 58 -102.72 -119.01
REMARK 500 3 SER A 59 135.12 -173.75
REMARK 500 3 MET A 84 -43.77 -144.06
REMARK 500 3 CYS A 107 144.48 67.82
REMARK 500 3 ALA A 109 4.43 -165.34
REMARK 500 3 SER A 113 -99.25 -170.93
REMARK 500 3 ALA A 117 -35.31 -138.03
REMARK 500 3 THR A 118 104.19 56.32
REMARK 500 3 PHE A 121 42.66 -80.05
REMARK 500 3 LEU A 138 -89.13 -58.75
REMARK 500 4 ALA A 33 23.44 46.76
REMARK 500 4 ILE A 34 111.17 63.70
REMARK 500 4 THR A 35 -159.42 -129.55
REMARK 500 4 GLN A 56 -147.68 -141.31
REMARK 500 4 ALA A 58 -101.64 -80.56
REMARK 500 4 SER A 59 136.76 -172.39
REMARK 500
REMARK 500 THIS ENTRY HAS 164 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 TWO ADDITIONAL C-TERMINAL RESIDUES (LE) RESULT FROM
REMARK 999 PRIMER DESIGN.
DBREF 1ZZP A 14 137 UNP P00519 ABL1_HUMAN 1007 1130
SEQADV 1ZZP GLY A 10 UNP P00519 CLONING ARTIFACT
SEQADV 1ZZP ALA A 11 UNP P00519 CLONING ARTIFACT
SEQADV 1ZZP MET A 12 UNP P00519 CLONING ARTIFACT
SEQADV 1ZZP ALA A 13 UNP P00519 CLONING ARTIFACT
SEQADV 1ZZP SER A 72 UNP P00519 THR 1065 VARIANT
SEQADV 1ZZP LEU A 138 UNP P00519 SEE REMARK 999
SEQADV 1ZZP GLU A 139 UNP P00519 SEE REMARK 999
SEQRES 1 A 130 GLY ALA MET ALA SER THR ARG VAL SER LEU ARG LYS THR
SEQRES 2 A 130 ARG GLN PRO PRO GLU ARG ILE ALA SER GLY ALA ILE THR
SEQRES 3 A 130 LYS GLY VAL VAL LEU ASP SER THR GLU ALA LEU CYS LEU
SEQRES 4 A 130 ALA ILE SER ARG ASN SER GLU GLN MET ALA SER HIS SER
SEQRES 5 A 130 ALA VAL LEU GLU ALA GLY LYS ASN LEU TYR SER PHE CYS
SEQRES 6 A 130 VAL SER TYR VAL ASP SER ILE GLN GLN MET ARG ASN LYS
SEQRES 7 A 130 PHE ALA PHE ARG GLU ALA ILE ASN LYS LEU GLU ASN ASN
SEQRES 8 A 130 LEU ARG GLU LEU GLN ILE CYS PRO ALA THR ALA GLY SER
SEQRES 9 A 130 GLY PRO ALA ALA THR GLN ASP PHE SER LYS LEU LEU SER
SEQRES 10 A 130 SER VAL LYS GLU ILE SER ASP ILE VAL GLN ARG LEU GLU
HELIX 1 1 THR A 35 ASN A 53 1 19
HELIX 2 2 SER A 59 VAL A 78 1 20
HELIX 3 3 ASP A 79 ILE A 81 5 3
HELIX 4 4 ASN A 86 GLN A 105 1 20
HELIX 5 5 PHE A 121 GLN A 136 1 16
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