Header list of 2dav.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN, CONTRACTILE PROTEIN 14-DEC-05 2DAV
TITLE SOLUTION STRUCTURE OF THE FIRST IG-LIKE DOMAIN OF MYOSIN-BINDING
TITLE 2 PROTEIN C, SLOW-TYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-BINDING PROTEIN C, SLOW-TYPE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IG DOMAIN;
COMPND 5 SYNONYM: SLOW MYBP-C; C-PROTEIN, SKELETAL MUSCLE SLOW-ISOFORM;
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: MYBPC1, MYBPCS;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050302-60;
SOURCE 9 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS IG DOMAIN, MYOSIN-BINDING PROTEIN C, SLOW-TYPE, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 STRUCTURAL PROTEIN, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DAV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DAV 1 VERSN
REVDAT 1 14-JUN-06 2DAV 0
JRNL AUTH X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST IG-LIKE DOMAIN OF
JRNL TITL 2 MYOSIN-BINDING PROTEIN C, SLOW-TYPE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DAV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025196.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.32MM 13C,15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9296, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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 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 SER A 2 52.23 -96.14
REMARK 500 1 PHE A 10 83.77 -59.76
REMARK 500 1 ILE A 11 -75.84 -33.28
REMARK 500 1 PRO A 14 94.72 -69.74
REMARK 500 1 LYS A 58 -75.53 -129.33
REMARK 500 1 ASP A 98 -74.16 -58.53
REMARK 500 1 THR A 116 146.15 -35.57
REMARK 500 2 PHE A 10 101.93 -37.04
REMARK 500 2 ILE A 11 -75.28 -71.84
REMARK 500 2 PRO A 14 85.06 -69.75
REMARK 500 2 GLN A 15 107.44 -56.33
REMARK 500 2 ALA A 56 109.57 -55.79
REMARK 500 2 LYS A 58 -52.55 -121.16
REMARK 500 2 ASP A 98 -70.64 -66.16
REMARK 500 2 ASN A 118 161.31 -49.16
REMARK 500 3 ASP A 98 -74.33 -63.48
REMARK 500 4 PHE A 10 76.05 -66.54
REMARK 500 4 ILE A 11 -76.07 -45.45
REMARK 500 4 PRO A 14 82.71 -69.71
REMARK 500 4 GLU A 34 -48.43 -132.23
REMARK 500 4 LYS A 58 -63.08 -132.20
REMARK 500 4 LYS A 97 -74.75 -27.82
REMARK 500 5 SER A 3 81.60 -66.51
REMARK 500 5 ILE A 8 118.74 -166.50
REMARK 500 5 PHE A 10 84.71 -54.26
REMARK 500 5 GLU A 34 -43.88 -133.81
REMARK 500 5 LYS A 58 -63.68 -123.07
REMARK 500 5 ASP A 98 -72.54 -64.69
REMARK 500 5 SER A 121 166.13 -46.67
REMARK 500 6 ILE A 11 -75.07 -41.84
REMARK 500 6 PRO A 14 83.11 -69.78
REMARK 500 6 ASP A 98 -73.43 -63.60
REMARK 500 7 PHE A 10 76.13 -62.19
REMARK 500 7 LYS A 48 -60.25 -102.91
REMARK 500 7 LYS A 58 -58.24 -129.86
REMARK 500 7 ASP A 98 -70.19 -65.02
REMARK 500 7 PRO A 123 -179.72 -69.77
REMARK 500 8 SER A 5 178.84 -50.12
REMARK 500 8 ILE A 11 -75.06 -33.97
REMARK 500 8 GLN A 15 39.25 -82.12
REMARK 500 8 ALA A 82 105.67 -54.09
REMARK 500 8 LYS A 97 -71.95 -33.30
REMARK 500 8 PRO A 117 -176.63 -69.78
REMARK 500 8 SER A 125 45.15 39.69
REMARK 500 9 PRO A 14 97.64 -69.78
REMARK 500 9 LYS A 58 -72.07 -129.06
REMARK 500 9 ASP A 98 -70.80 -72.07
REMARK 500 9 PRO A 123 -177.09 -69.74
REMARK 500 10 LEU A 9 75.68 -112.88
REMARK 500 10 ILE A 11 -75.07 -61.72
REMARK 500
REMARK 500 THIS ENTRY HAS 110 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002000567.2 RELATED DB: TARGETDB
DBREF 2DAV A 8 120 UNP Q00872 MYPC1_HUMAN 58 170
SEQADV 2DAV GLY A 1 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV SER A 2 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV SER A 3 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV GLY A 4 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV SER A 5 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV SER A 6 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV GLY A 7 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV SER A 121 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV GLY A 122 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV PRO A 123 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV SER A 124 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV SER A 125 UNP Q00872 CLONING ARTIFACT
SEQADV 2DAV GLY A 126 UNP Q00872 CLONING ARTIFACT
SEQRES 1 A 126 GLY SER SER GLY SER SER GLY ILE LEU PHE ILE GLU LYS
SEQRES 2 A 126 PRO GLN GLY GLY THR VAL LYS VAL GLY GLU ASP ILE THR
SEQRES 3 A 126 PHE ILE ALA LYS VAL LYS ALA GLU ASP LEU LEU ARG LYS
SEQRES 4 A 126 PRO THR ILE LYS TRP PHE LYS GLY LYS TRP MET ASP LEU
SEQRES 5 A 126 ALA SER LYS ALA GLY LYS HIS LEU GLN LEU LYS GLU THR
SEQRES 6 A 126 PHE GLU ARG HIS SER ARG VAL TYR THR PHE GLU MET GLN
SEQRES 7 A 126 ILE ILE LYS ALA LYS ASP ASN PHE ALA GLY ASN TYR ARG
SEQRES 8 A 126 CYS GLU VAL THR TYR LYS ASP LYS PHE ASP SER CYS SER
SEQRES 9 A 126 PHE ASP LEU GLU VAL HIS GLU SER THR GLY THR THR PRO
SEQRES 10 A 126 ASN ILE ASP SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 51 ALA A 56 1 6
SHEET 1 A 4 THR A 18 LYS A 20 0
SHEET 2 A 4 ASP A 106 HIS A 110 1 O GLU A 108 N VAL A 19
SHEET 3 A 4 GLY A 88 THR A 95 -1 N GLY A 88 O LEU A 107
SHEET 4 A 4 THR A 41 LYS A 46 -1 N PHE A 45 O ARG A 91
SHEET 1 B 4 THR A 18 LYS A 20 0
SHEET 2 B 4 ASP A 106 HIS A 110 1 O GLU A 108 N VAL A 19
SHEET 3 B 4 GLY A 88 THR A 95 -1 N GLY A 88 O LEU A 107
SHEET 4 B 4 PHE A 100 CYS A 103 -1 O ASP A 101 N VAL A 94
SHEET 1 C 3 ILE A 25 LYS A 32 0
SHEET 2 C 3 VAL A 72 ILE A 79 -1 O PHE A 75 N ALA A 29
SHEET 3 C 3 LEU A 60 GLU A 67 -1 N THR A 65 O THR A 74
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