Header list of 1ark.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSFERASE 07-AUG-97 1ARK
TITLE SH3 DOMAIN FROM HUMAN NEBULIN, NMR, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEBULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 6610 - 6669;
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 CELL_LINE: BL21 (DE3) PLYSS;
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_CELL_LINE: BL21 (DE3) PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS TRANSFERASE, SH3 DOMAIN, NEBULIN, Z-DISK ASSEMBLY, ACTIN-BINDING
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR A.S.POLITOU,A.PASTORE
REVDAT 3 16-FEB-22 1ARK 1 REMARK
REVDAT 2 24-FEB-09 1ARK 1 VERSN
REVDAT 1 28-JAN-98 1ARK 0
JRNL AUTH A.S.POLITOU,S.MILLEVOI,M.GAUTEL,B.KOLMERER,A.PASTORE
JRNL TITL SH3 IN MUSCLES: SOLUTION STRUCTURE OF THE SH3 DOMAIN FROM
JRNL TITL 2 NEBULIN.
JRNL REF J.MOL.BIOL. V. 276 189 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9514727
JRNL DOI 10.1006/JMBI.1997.1521
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ARK 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_1000171170.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BRUKER UXNMR UXNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 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 ILE A 5 169.56 54.91
REMARK 500 1 ASP A 16 -155.86 -147.69
REMARK 500 1 GLU A 19 -168.62 -103.35
REMARK 500 1 ILE A 29 -135.24 -106.62
REMARK 500 1 ASN A 30 79.29 -169.03
REMARK 500 1 ALA A 33 103.70 -172.22
REMARK 500 1 ASP A 35 155.53 59.99
REMARK 500 1 GLU A 36 38.85 38.28
REMARK 500 1 VAL A 43 107.68 -55.84
REMARK 500 1 THR A 46 -47.30 -140.05
REMARK 500 2 ALA A 2 -150.20 53.27
REMARK 500 2 ILE A 29 -143.12 -126.98
REMARK 500 2 ASN A 30 76.82 -157.15
REMARK 500 2 GLN A 32 -72.25 -133.45
REMARK 500 2 ALA A 33 116.18 59.86
REMARK 500 2 ASP A 35 -177.43 -177.81
REMARK 500 2 TRP A 38 140.07 59.67
REMARK 500 2 TYR A 56 -62.60 -95.27
REMARK 500 3 ALA A 2 -82.42 -105.55
REMARK 500 3 LYS A 4 -170.45 45.14
REMARK 500 3 VAL A 20 -151.81 -120.11
REMARK 500 3 ILE A 29 -156.53 -64.74
REMARK 500 3 ILE A 34 -72.05 -59.80
REMARK 500 3 ASP A 35 -63.74 -176.37
REMARK 500 3 TRP A 38 170.99 55.25
REMARK 500 3 THR A 46 -68.16 -92.11
REMARK 500 4 LYS A 4 -169.43 -77.83
REMARK 500 4 ILE A 29 -159.19 -73.71
REMARK 500 4 VAL A 31 -80.96 -73.43
REMARK 500 4 ILE A 34 -80.38 -73.16
REMARK 500 4 ASP A 35 18.07 -169.53
REMARK 500 4 TYR A 56 -40.15 -131.78
REMARK 500 5 ILE A 5 141.59 61.25
REMARK 500 5 GLU A 19 -165.46 -118.14
REMARK 500 5 ALA A 33 80.76 53.31
REMARK 500 5 ASP A 35 -69.92 65.42
REMARK 500 5 TRP A 38 179.04 52.56
REMARK 500 5 VAL A 43 97.45 -61.98
REMARK 500 5 ARG A 48 -168.93 -70.54
REMARK 500 6 LYS A 4 -171.59 -69.58
REMARK 500 6 ASP A 11 71.63 60.36
REMARK 500 6 ASP A 16 -151.03 -95.77
REMARK 500 6 ILE A 29 -169.84 -58.88
REMARK 500 6 VAL A 31 -158.42 -80.84
REMARK 500 6 GLN A 32 -156.89 -160.49
REMARK 500 6 ALA A 33 -152.46 -137.23
REMARK 500 6 ILE A 34 -85.79 -128.45
REMARK 500 6 ASP A 35 -64.20 -108.81
REMARK 500 6 MET A 39 -152.13 -146.30
REMARK 500 6 ARG A 45 -71.56 -75.85
REMARK 500
REMARK 500 THIS ENTRY HAS 126 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 7 0.32 SIDE CHAIN
REMARK 500 1 ARG A 45 0.17 SIDE CHAIN
REMARK 500 1 ARG A 48 0.30 SIDE CHAIN
REMARK 500 2 ARG A 7 0.29 SIDE CHAIN
REMARK 500 2 ARG A 45 0.31 SIDE CHAIN
REMARK 500 2 ARG A 48 0.29 SIDE CHAIN
REMARK 500 3 ARG A 7 0.30 SIDE CHAIN
REMARK 500 3 ARG A 45 0.25 SIDE CHAIN
REMARK 500 3 ARG A 48 0.23 SIDE CHAIN
REMARK 500 4 ARG A 7 0.25 SIDE CHAIN
REMARK 500 4 ARG A 45 0.28 SIDE CHAIN
REMARK 500 4 ARG A 48 0.14 SIDE CHAIN
REMARK 500 5 ARG A 7 0.30 SIDE CHAIN
REMARK 500 5 ARG A 45 0.20 SIDE CHAIN
REMARK 500 5 ARG A 48 0.30 SIDE CHAIN
REMARK 500 6 ARG A 7 0.28 SIDE CHAIN
REMARK 500 6 ARG A 45 0.08 SIDE CHAIN
REMARK 500 6 ARG A 48 0.26 SIDE CHAIN
REMARK 500 7 ARG A 7 0.32 SIDE CHAIN
REMARK 500 7 ARG A 45 0.16 SIDE CHAIN
REMARK 500 7 ARG A 48 0.18 SIDE CHAIN
REMARK 500 8 ARG A 7 0.31 SIDE CHAIN
REMARK 500 8 ARG A 45 0.24 SIDE CHAIN
REMARK 500 8 ARG A 48 0.30 SIDE CHAIN
REMARK 500 9 ARG A 7 0.23 SIDE CHAIN
REMARK 500 9 ARG A 45 0.23 SIDE CHAIN
REMARK 500 9 ARG A 48 0.29 SIDE CHAIN
REMARK 500 10 ARG A 7 0.16 SIDE CHAIN
REMARK 500 10 ARG A 45 0.30 SIDE CHAIN
REMARK 500 10 ARG A 48 0.32 SIDE CHAIN
REMARK 500 11 ARG A 7 0.17 SIDE CHAIN
REMARK 500 11 ARG A 45 0.20 SIDE CHAIN
REMARK 500 11 ARG A 48 0.31 SIDE CHAIN
REMARK 500 12 ARG A 7 0.18 SIDE CHAIN
REMARK 500 12 ARG A 45 0.30 SIDE CHAIN
REMARK 500 12 ARG A 48 0.32 SIDE CHAIN
REMARK 500 13 ARG A 7 0.28 SIDE CHAIN
REMARK 500 13 ARG A 45 0.32 SIDE CHAIN
REMARK 500 13 ARG A 48 0.30 SIDE CHAIN
REMARK 500 14 ARG A 7 0.24 SIDE CHAIN
REMARK 500 14 ARG A 45 0.31 SIDE CHAIN
REMARK 500 14 ARG A 48 0.32 SIDE CHAIN
REMARK 500 15 ARG A 7 0.28 SIDE CHAIN
REMARK 500 15 ARG A 45 0.28 SIDE CHAIN
REMARK 500 15 ARG A 48 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ARK A 1 60 UNP P20929 NEBU_HUMAN 918 977
SEQRES 1 A 60 THR ALA GLY LYS ILE PHE ARG ALA MET TYR ASP TYR MET
SEQRES 2 A 60 ALA ALA ASP ALA ASP GLU VAL SER PHE LYS ASP GLY ASP
SEQRES 3 A 60 ALA ILE ILE ASN VAL GLN ALA ILE ASP GLU GLY TRP MET
SEQRES 4 A 60 TYR GLY THR VAL GLN ARG THR GLY ARG THR GLY MET LEU
SEQRES 5 A 60 PRO ALA ASN TYR VAL GLU ALA ILE
HELIX 1 H ALA A 54 TYR A 56 5ONE TURN 3
SHEET 1 B1 1 PHE A 6 MET A 9 0
SHEET 1 B2 1 GLN A 32 ILE A 34 0
SHEET 1 C1 1 ALA A 27 ILE A 29 0
SHEET 1 C2 1 TRP A 38 VAL A 43 0
SHEET 1 D1 1 VAL A 57 ILE A 60 0
SHEET 1 D2 1 ARG A 48 PRO A 53 0
SHEET 1 B3 2 ASP A 11 ALA A 14 0
SHEET 2 B3 2 SER A 21 ASP A 24 0
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