Header list of 1aj3.pdb file
Complete list - b 16 2 Bytes
HEADER CYTOSKELETON 14-MAY-97 1AJ3
TITLE SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA SPECTRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 16TH REPEAT, RESIDUES 1772 - 1869;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: BRAIN;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-3D
KEYWDS ELASTICITY, MEMBRANE SKELETON, SPECTRIN, COILED-COIL, CYTOSKELETON,
KEYWDS 2 CALMODULIN-BINDING, ACTIN-BINDING, CAPPING PROTEIN, CALCIUM-BINDING,
KEYWDS 3 DUPLICATION, SH3 DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.PASCUAL,M.PFUHL,D.WALTHER,M.SARASTE,M.NILGES
REVDAT 3 16-FEB-22 1AJ3 1 REMARK
REVDAT 2 24-FEB-09 1AJ3 1 VERSN
REVDAT 1 07-JUL-97 1AJ3 0
JRNL AUTH J.PASCUAL,M.PFUHL,D.WALTHER,M.SARASTE,M.NILGES
JRNL TITL SOLUTION STRUCTURE OF THE SPECTRIN REPEAT: A LEFT-HANDED
JRNL TITL 2 ANTIPARALLEL TRIPLE-HELICAL COILED-COIL.
JRNL REF J.MOL.BIOL. V. 273 740 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9356261
JRNL DOI 10.1006/JMBI.1997.1344
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : A. BRUNGER, M. NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AMBIGUOUS RESTRAINTS FOR ITERATIVE
REMARK 3 ASSIGNMENT METHOD (ARIA) DIRECT REFINEMENT AGAINST 1H-CHEMICAL
REMARK 3 SHIFTS
REMARK 4
REMARK 4 1AJ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170878.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HN(CO)CA; HNCO; HN (CA)CO;
REMARK 210 HCCH-COSY; HCCH-TOCSY; 15N; 13C
REMARK 210 HSQC-NOESY
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 : AZARA
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY, GEOMETRY, VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 LYS A 2
REMARK 465 LEU A 3
REMARK 465 ASN A 4
REMARK 465 GLU A 5
REMARK 465 SER A 6
REMARK 465 HIS A 7
REMARK 465 ARG A 8
REMARK 465 LEU A 9
REMARK 465 ARG A 108
REMARK 465 LEU A 109
REMARK 465 GLU A 110
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 10 PHE A 91 CE1 PHE A 91 CZ 0.117
REMARK 500 18 PHE A 91 CE1 PHE A 91 CZ 0.157
REMARK 500 18 PHE A 91 CZ PHE A 91 CE2 -0.139
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 ASP A 34 -45.66 -133.90
REMARK 500 1 ARG A 37 118.70 71.32
REMARK 500 1 ASN A 77 -59.00 -153.10
REMARK 500 1 THR A 78 -70.33 70.85
REMARK 500 1 ILE A 79 93.11 -57.72
REMARK 500 2 GLU A 33 -49.35 135.95
REMARK 500 2 LEU A 39 42.48 88.51
REMARK 500 3 ASP A 34 129.54 66.85
REMARK 500 3 ARG A 37 54.33 24.01
REMARK 500 3 THR A 78 -73.89 -58.10
REMARK 500 4 TYR A 35 -12.29 72.71
REMARK 500 4 THR A 40 29.31 -153.07
REMARK 500 4 ASN A 77 37.86 79.01
REMARK 500 5 LEU A 39 30.57 87.68
REMARK 500 5 ASP A 76 -37.15 145.57
REMARK 500 5 THR A 78 108.83 64.26
REMARK 500 6 ARG A 37 -74.49 -162.06
REMARK 500 6 ASP A 38 19.24 45.79
REMARK 500 6 LEU A 39 17.91 52.78
REMARK 500 6 THR A 40 54.26 -168.05
REMARK 500 6 ILE A 79 59.89 -92.01
REMARK 500 7 GLU A 33 29.44 -77.13
REMARK 500 7 TYR A 35 -15.85 -176.52
REMARK 500 7 ARG A 37 -39.65 -29.20
REMARK 500 7 ASP A 38 28.18 44.19
REMARK 500 7 LEU A 39 23.44 49.18
REMARK 500 7 THR A 40 86.18 -171.12
REMARK 500 7 ASN A 77 59.60 77.29
REMARK 500 7 ILE A 79 96.37 -66.41
REMARK 500 8 ASP A 34 17.53 56.12
REMARK 500 8 ARG A 37 88.02 56.09
REMARK 500 8 THR A 78 -65.23 73.86
REMARK 500 9 ARG A 37 85.45 -153.63
REMARK 500 9 ASP A 38 -74.73 -19.69
REMARK 500 9 THR A 40 55.89 -140.66
REMARK 500 10 TYR A 35 -66.61 -163.71
REMARK 500 10 LEU A 39 18.25 -69.90
REMARK 500 10 THR A 40 13.23 -152.87
REMARK 500 10 ASN A 77 87.58 -158.11
REMARK 500 10 ILE A 79 -63.58 -141.03
REMARK 500 11 GLU A 33 -66.41 73.39
REMARK 500 11 ASP A 34 -79.39 -147.97
REMARK 500 11 ARG A 37 -53.01 -174.99
REMARK 500 11 ASP A 38 4.39 58.84
REMARK 500 11 THR A 40 99.10 -169.96
REMARK 500 11 ASN A 77 -32.23 179.82
REMARK 500 11 ILE A 79 91.92 -63.03
REMARK 500 12 TYR A 35 -99.87 29.51
REMARK 500 12 ASP A 38 31.98 -87.62
REMARK 500 12 LEU A 39 -18.74 -143.38
REMARK 500
REMARK 500 THIS ENTRY HAS 83 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AJ3 A 1 110 UNP P07751 SPTA2_CHICK 1763 1872
SEQRES 1 A 110 ALA LYS LEU ASN GLU SER HIS ARG LEU HIS GLN PHE PHE
SEQRES 2 A 110 ARG ASP MET ASP ASP GLU GLU SER TRP ILE LYS GLU LYS
SEQRES 3 A 110 LYS LEU LEU VAL SER SER GLU ASP TYR GLY ARG ASP LEU
SEQRES 4 A 110 THR GLY VAL GLN ASN LEU ARG LYS LYS HIS LYS ARG LEU
SEQRES 5 A 110 GLU ALA GLU LEU ALA ALA HIS GLU PRO ALA ILE GLN GLY
SEQRES 6 A 110 VAL LEU ASP THR GLY LYS LYS LEU SER ASP ASP ASN THR
SEQRES 7 A 110 ILE GLY LYS GLU GLU ILE GLN GLN ARG LEU ALA GLN PHE
SEQRES 8 A 110 VAL ASP HIS TRP LYS GLU LEU LYS GLN LEU ALA ALA ALA
SEQRES 9 A 110 ARG GLY GLN ARG LEU GLU
HELIX 1 1 GLN A 11 SER A 32 1 22
HELIX 2 2 ASP A 38 ASP A 76 1 39
HELIX 3 3 LYS A 81 ARG A 105 1 25
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 - b 16 2 Bytes