Header list of 1gxe.pdb file
Complete list - r 28 2 Bytes
HEADER CYTOSKELETON 03-APR-02 1GXE
TITLE CENTRAL DOMAIN OF CARDIAC MYOSIN BINDING PROTEIN C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN BINDING PROTEIN C, CARDIAC-TYPE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN C5, RESIDUES 641-770;
COMPND 5 SYNONYM: CARDIAC MYBP-C, C-PROTEIN - CARDIAC MUSCLE ISOFORM;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: HIS-TAGGED PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: HEART;
SOURCE 6 TISSUE: MUSCLE;
SOURCE 7 CELL: MYOCYTE;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET8C;
SOURCE 11 OTHER_DETAILS: CARDIAC PROTEIN
KEYWDS CYTOSKELETON, MUSCLE, IGI, THICK FILAMENT, IMMUNOGLOBULIN DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.PFUHL
REVDAT 3 28-MAR-18 1GXE 1 TITLE SOURCE REMARK
REVDAT 2 24-FEB-09 1GXE 1 VERSN
REVDAT 1 12-JUN-03 1GXE 0
JRNL AUTH S.IDOWU,M.GAUTEL,S.PERKINS,M.PFUHL
JRNL TITL STRUCTURE, STABILITY AND DYNAMICS OF THE CENTRAL DOMAIN OF
JRNL TITL 2 CARDIAC MYOSIN BINDING PROTEIN C (MYBP-C): IMPLICATIONS FOR
JRNL TITL 3 MULTIDOMAIN ASSEMBLY AND CAUSES FOR CARDIOMYOPATHY
JRNL REF J.MOL.BIOL. V. 329 745 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12787675
JRNL DOI 10.1016/S0022-2836(03)00425-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.IDOWU,M.GAUTEL,M.PFUHL
REMARK 1 TITL SEQUENCE SPECIFIC RESONANCE ASSIGNMENT OF THE CENTRAL DOMAIN
REMARK 1 TITL 2 OF CARDIAC MYOSIN BINDING PROTEIN C (MYBP-C)
REMARK 1 REF J.BIOMOL.NMR V. 22 199 2002
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 11883787
REMARK 1 DOI 10.1023/A:1014248522896
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING WITH STANDARD XPLOR
REMARK 3 PROTOCOL DESCRIBED IN MANUSCRIPT. RESIDUES -9 TO -1 CONSTITUTE A
REMARK 3 HIS-TAG. THESE RESIDUES WERE PRESENT IN THE EXPERIMENT BUT WERE
REMARK 3 NOT ASSIGNED NOR USED IN THE STRUCTURE CALCULATION.
REMARK 4
REMARK 4 1GXE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1290009594.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N NOESY-HSQC; 13C NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINT VIOLATIONS 0.2 A
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: 3D 15N NOESY-HSQC & 3D 13C NOESY-HSQC IN 90% H2O/10% D2O
REMARK 210 3D 13C NOESY-HSQC IN 99% D2O
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 MET A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 SER A -2
REMARK 465 SER A -1
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 TYR A 109 H LEU A 124 1.56
REMARK 500 O VAL A 21 H ILE A 129 1.58
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 GLN A 2 -132.90 -145.11
REMARK 500 1 LEU A 9 -92.48 -119.38
REMARK 500 1 CYS A 11 -61.77 -170.19
REMARK 500 1 ASP A 17 80.13 -65.56
REMARK 500 1 VAL A 22 54.80 -93.35
REMARK 500 1 ALA A 23 93.30 45.25
REMARK 500 1 SER A 34 -147.68 -81.14
REMARK 500 1 GLN A 49 -73.63 -97.54
REMARK 500 1 ASN A 51 -158.39 -154.66
REMARK 500 1 LYS A 52 -159.96 53.10
REMARK 500 1 ALA A 53 173.23 -51.59
REMARK 500 1 ARG A 56 73.85 -119.60
REMARK 500 1 ALA A 61 98.02 -42.61
REMARK 500 1 ASP A 67 30.73 -145.88
REMARK 500 1 TRP A 71 74.50 -104.69
REMARK 500 1 PHE A 73 -90.33 52.89
REMARK 500 1 ASP A 74 -163.99 -69.35
REMARK 500 1 LYS A 76 99.75 -62.29
REMARK 500 1 CYS A 79 -72.74 -83.32
REMARK 500 1 THR A 81 -162.42 -73.67
REMARK 500 1 THR A 90 -177.49 -67.80
REMARK 500 1 GLU A 99 43.93 -106.89
REMARK 500 1 LYS A 127 117.44 -164.02
REMARK 500 2 GLN A 2 -159.89 -61.38
REMARK 500 2 LYS A 6 149.63 -170.47
REMARK 500 2 ILE A 7 63.77 -68.81
REMARK 500 2 LEU A 9 -98.23 -124.11
REMARK 500 2 CYS A 11 -66.80 -153.66
REMARK 500 2 PRO A 12 -87.35 -68.51
REMARK 500 2 ASP A 17 79.91 -59.22
REMARK 500 2 ALA A 23 95.18 40.66
REMARK 500 2 SER A 34 -145.45 -72.79
REMARK 500 2 ASN A 51 -68.76 -129.51
REMARK 500 2 LYS A 52 -160.38 -126.91
REMARK 500 2 ARG A 56 73.80 -118.43
REMARK 500 2 ALA A 61 98.23 -42.94
REMARK 500 2 GLU A 63 78.73 -67.74
REMARK 500 2 ASP A 67 74.96 -152.02
REMARK 500 2 SER A 68 70.05 52.77
REMARK 500 2 ASP A 69 -87.04 55.40
REMARK 500 2 GLU A 70 -170.24 -65.21
REMARK 500 2 TRP A 71 77.38 -111.42
REMARK 500 2 PHE A 73 -164.16 37.52
REMARK 500 2 LYS A 75 177.96 -53.77
REMARK 500 2 LYS A 76 156.44 60.51
REMARK 500 2 LEU A 77 -177.16 -170.41
REMARK 500 2 CYS A 79 -176.73 -64.49
REMARK 500 2 THR A 81 -156.10 -172.77
REMARK 500 2 GLU A 82 -66.06 66.50
REMARK 500 2 ARG A 84 -79.70 -91.85
REMARK 500
REMARK 500 THIS ENTRY HAS 258 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 1 0.28 SIDE CHAIN
REMARK 500 1 ARG A 14 0.25 SIDE CHAIN
REMARK 500 1 ARG A 28 0.31 SIDE CHAIN
REMARK 500 1 ARG A 56 0.24 SIDE CHAIN
REMARK 500 1 ARG A 84 0.25 SIDE CHAIN
REMARK 500 1 ARG A 86 0.25 SIDE CHAIN
REMARK 500 1 ARG A 93 0.21 SIDE CHAIN
REMARK 500 2 ARG A 1 0.26 SIDE CHAIN
REMARK 500 2 ARG A 14 0.26 SIDE CHAIN
REMARK 500 2 ARG A 28 0.29 SIDE CHAIN
REMARK 500 2 ARG A 56 0.31 SIDE CHAIN
REMARK 500 2 ARG A 84 0.32 SIDE CHAIN
REMARK 500 2 ARG A 86 0.32 SIDE CHAIN
REMARK 500 2 ARG A 93 0.23 SIDE CHAIN
REMARK 500 3 ARG A 1 0.23 SIDE CHAIN
REMARK 500 3 ARG A 14 0.25 SIDE CHAIN
REMARK 500 3 ARG A 28 0.27 SIDE CHAIN
REMARK 500 3 ARG A 56 0.22 SIDE CHAIN
REMARK 500 3 ARG A 84 0.23 SIDE CHAIN
REMARK 500 3 ARG A 86 0.27 SIDE CHAIN
REMARK 500 3 ARG A 93 0.31 SIDE CHAIN
REMARK 500 4 ARG A 1 0.24 SIDE CHAIN
REMARK 500 4 ARG A 14 0.28 SIDE CHAIN
REMARK 500 4 ARG A 28 0.28 SIDE CHAIN
REMARK 500 4 ARG A 56 0.25 SIDE CHAIN
REMARK 500 4 ARG A 84 0.29 SIDE CHAIN
REMARK 500 4 ARG A 86 0.32 SIDE CHAIN
REMARK 500 4 ARG A 93 0.25 SIDE CHAIN
REMARK 500 5 ARG A 1 0.31 SIDE CHAIN
REMARK 500 5 ARG A 14 0.29 SIDE CHAIN
REMARK 500 5 ARG A 28 0.26 SIDE CHAIN
REMARK 500 5 ARG A 56 0.24 SIDE CHAIN
REMARK 500 5 ARG A 84 0.30 SIDE CHAIN
REMARK 500 5 ARG A 86 0.28 SIDE CHAIN
REMARK 500 5 ARG A 93 0.25 SIDE CHAIN
REMARK 500 6 ARG A 1 0.29 SIDE CHAIN
REMARK 500 6 ARG A 14 0.28 SIDE CHAIN
REMARK 500 6 ARG A 28 0.22 SIDE CHAIN
REMARK 500 6 ARG A 56 0.23 SIDE CHAIN
REMARK 500 6 ARG A 84 0.24 SIDE CHAIN
REMARK 500 6 ARG A 86 0.32 SIDE CHAIN
REMARK 500 6 ARG A 93 0.26 SIDE CHAIN
REMARK 500 7 ARG A 1 0.28 SIDE CHAIN
REMARK 500 7 ARG A 14 0.23 SIDE CHAIN
REMARK 500 7 ARG A 28 0.21 SIDE CHAIN
REMARK 500 7 ARG A 56 0.25 SIDE CHAIN
REMARK 500 7 ARG A 84 0.24 SIDE CHAIN
REMARK 500 7 ARG A 86 0.32 SIDE CHAIN
REMARK 500 7 ARG A 93 0.29 SIDE CHAIN
REMARK 500 8 ARG A 1 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 70 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GXE A -9 -1 PDB 1GXE 1GXE -9 -1
DBREF 1GXE A 1 130 UNP Q14896 MYPC_HUMAN 641 770
SEQRES 1 A 139 MET HIS HIS HIS HIS HIS HIS SER SER ARG GLN GLU PRO
SEQRES 2 A 139 PRO LYS ILE HIS LEU ASP CYS PRO GLY ARG ILE PRO ASP
SEQRES 3 A 139 THR ILE VAL VAL VAL ALA GLY ASN LYS LEU ARG LEU ASP
SEQRES 4 A 139 VAL PRO ILE SER GLY ASP PRO ALA PRO THR VAL ILE TRP
SEQRES 5 A 139 GLN LYS ALA ILE THR GLN GLY ASN LYS ALA PRO ALA ARG
SEQRES 6 A 139 PRO ALA PRO ASP ALA PRO GLU ASP THR GLY ASP SER ASP
SEQRES 7 A 139 GLU TRP VAL PHE ASP LYS LYS LEU LEU CYS GLU THR GLU
SEQRES 8 A 139 GLY ARG VAL ARG VAL GLU THR THR LYS ASP ARG SER ILE
SEQRES 9 A 139 PHE THR VAL GLU GLY ALA GLU LYS GLU ASP GLU GLY VAL
SEQRES 10 A 139 TYR THR VAL THR VAL LYS ASN PRO VAL GLY GLU ASP GLN
SEQRES 11 A 139 VAL ASN LEU THR VAL LYS VAL ILE ASP
SHEET 1 AA 4 THR A 18 VAL A 21 0
SHEET 2 AA 4 GLU A 119 VAL A 128 1 O THR A 125 N ILE A 19
SHEET 3 AA 4 GLY A 107 LYS A 114 -1 O GLY A 107 N VAL A 126
SHEET 4 AA 4 THR A 40 ALA A 46 -1 N THR A 40 O LYS A 114
SHEET 1 AB 3 ASP A 30 PRO A 32 0
SHEET 2 AB 3 ARG A 93 THR A 97 -1 O SER A 94 N VAL A 31
SHEET 3 AB 3 ARG A 86 THR A 90 -1 O ARG A 86 N THR A 97
CISPEP 1 ASP A 36 PRO A 37 1 -0.24
CISPEP 2 ASP A 36 PRO A 37 2 0.16
CISPEP 3 ASP A 36 PRO A 37 3 -0.29
CISPEP 4 ASP A 36 PRO A 37 4 0.08
CISPEP 5 ASP A 36 PRO A 37 5 0.12
CISPEP 6 ASP A 36 PRO A 37 6 -0.32
CISPEP 7 ASP A 36 PRO A 37 7 -0.20
CISPEP 8 ASP A 36 PRO A 37 8 0.50
CISPEP 9 ASP A 36 PRO A 37 9 -0.03
CISPEP 10 ASP A 36 PRO A 37 10 0.37
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 28 2 Bytes