Header list of 1x44.pdb file
Complete list - r 2 2 Bytes
HEADER CONTRACTILE PROTEIN 13-MAY-05 1X44
TITLE SOLUTION STRUCTURE OF THE THIRD IG-LIKE DOMAIN OF MYOSIN-DINDING
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-LIKE 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_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050125-02;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS IG-LIKE DOMAIN, MYOSIN-BINDING PROTEIN C, SLOW-TYPE/SKELETAL MUSCLE
KEYWDS 2 SLOW-ISOFORM, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 3 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.-R.QIN,C.KUROSAKI,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X44 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X44 1 VERSN
REVDAT 1 13-NOV-05 1X44 0
JRNL AUTH X.-R.QIN,C.KUROSAKI,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE THIRD IG-LIKE DOMAIN OF
JRNL TITL 2 MYOSIN-DINDING 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 1X44 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024354.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.14MM 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: SPECTROMETER_ID 1 FOR 3D_15N_SEPARATED_NOESY;
REMARK 210 SPECTROMETER_ID 2 FOR 3D_13C_SEPARATED_NOESY
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 5 156.95 -38.06
REMARK 500 1 SER A 6 -74.65 -52.53
REMARK 500 1 ASP A 35 39.87 34.49
REMARK 500 1 PRO A 49 -165.21 -69.77
REMARK 500 1 ALA A 76 94.47 -61.94
REMARK 500 1 LYS A 97 122.33 -36.56
REMARK 500 2 ASP A 35 41.42 34.78
REMARK 500 2 PRO A 49 -177.11 -69.78
REMARK 500 2 ALA A 76 92.07 -45.26
REMARK 500 3 SER A 5 114.72 -174.62
REMARK 500 3 ASP A 35 40.60 35.52
REMARK 500 3 SER A 53 163.99 -45.45
REMARK 500 3 ALA A 76 90.53 -63.83
REMARK 500 4 ASP A 35 49.98 38.37
REMARK 500 4 PRO A 49 -176.53 -69.77
REMARK 500 4 LYS A 52 -35.11 -130.62
REMARK 500 4 ALA A 76 95.78 -51.89
REMARK 500 4 PRO A 100 90.41 -69.81
REMARK 500 5 CYS A 21 108.70 -57.16
REMARK 500 5 ASP A 35 41.26 35.14
REMARK 500 5 PRO A 49 -173.44 -69.81
REMARK 500 5 ALA A 76 89.05 -58.98
REMARK 500 6 ASP A 35 37.78 37.57
REMARK 500 6 PRO A 49 -174.18 -69.80
REMARK 500 6 ALA A 76 91.69 -67.91
REMARK 500 7 SER A 3 110.42 -38.45
REMARK 500 7 ASP A 35 46.33 34.98
REMARK 500 7 PRO A 49 -176.94 -69.78
REMARK 500 7 ALA A 76 90.74 -48.07
REMARK 500 7 LYS A 97 108.12 -59.41
REMARK 500 8 SER A 3 143.50 -172.08
REMARK 500 8 SER A 6 105.44 -42.57
REMARK 500 8 ASP A 16 137.03 -34.43
REMARK 500 8 CYS A 21 108.57 -54.40
REMARK 500 8 ASP A 35 37.42 35.43
REMARK 500 8 ASN A 37 87.94 -52.83
REMARK 500 8 PRO A 49 -166.92 -69.75
REMARK 500 8 LYS A 52 42.72 -106.58
REMARK 500 8 ALA A 76 93.13 -50.41
REMARK 500 9 SER A 3 95.66 -56.83
REMARK 500 9 ASP A 34 174.67 -57.40
REMARK 500 9 ASP A 35 43.03 38.46
REMARK 500 9 ASN A 37 90.65 -57.62
REMARK 500 9 PRO A 49 -179.62 -69.78
REMARK 500 9 PRO A 51 2.50 -69.75
REMARK 500 9 LYS A 52 -35.11 -132.87
REMARK 500 9 SER A 53 174.94 -47.23
REMARK 500 9 ALA A 76 91.10 -46.14
REMARK 500 9 SER A 101 127.00 -34.65
REMARK 500 10 ASP A 35 51.06 35.78
REMARK 500
REMARK 500 THIS ENTRY HAS 107 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002000567.1 RELATED DB: TARGETDB
DBREF 1X44 A 8 97 UNP Q00872 MYPC1_HUMAN 342 431
SEQADV 1X44 GLY A 1 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 SER A 2 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 SER A 3 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 GLY A 4 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 SER A 5 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 SER A 6 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 GLY A 7 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 SER A 98 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 GLY A 99 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 PRO A 100 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 SER A 101 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 SER A 102 UNP Q00872 CLONING ARTIFACT
SEQADV 1X44 GLY A 103 UNP Q00872 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY ILE MET VAL THR LYS GLN
SEQRES 2 A 103 LEU GLU ASP THR THR ALA TYR CYS GLY GLU ARG VAL GLU
SEQRES 3 A 103 LEU GLU CYS GLU VAL SER GLU ASP ASP ALA ASN VAL LYS
SEQRES 4 A 103 TRP PHE LYS ASN GLY GLU GLU ILE ILE PRO GLY PRO LYS
SEQRES 5 A 103 SER ARG TYR ARG ILE ARG VAL GLU GLY LYS LYS HIS ILE
SEQRES 6 A 103 LEU ILE ILE GLU GLY ALA THR LYS ALA ASP ALA ALA GLU
SEQRES 7 A 103 TYR SER VAL MET THR THR GLY GLY GLN SER SER ALA LYS
SEQRES 8 A 103 LEU SER VAL ASP LEU LYS SER GLY PRO SER SER GLY
SHEET 1 A 5 THR A 17 TYR A 20 0
SHEET 2 A 5 GLY A 86 ASP A 95 1 O ASP A 95 N ALA A 19
SHEET 3 A 5 GLU A 78 THR A 83 -1 N THR A 83 O GLY A 86
SHEET 4 A 5 LYS A 39 LYS A 42 -1 N PHE A 41 O SER A 80
SHEET 5 A 5 GLU A 45 GLU A 46 -1 O GLU A 45 N LYS A 42
SHEET 1 B 3 GLU A 23 GLU A 30 0
SHEET 2 B 3 LYS A 63 ALA A 71 -1 O ALA A 71 N GLU A 23
SHEET 3 B 3 TYR A 55 GLU A 60 -1 N GLU A 60 O LYS A 63
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 2 2 Bytes