Header list of 2cqv.pdb file
Complete list - r 9 2 Bytes
HEADER CONTRACTILE PROTEIN 20-MAY-05 2CQV
TITLE SOLUTION STRUCTURE OF THE EIGHTH IG-LIKE DOMAIN OF HUMAN MYOSIN LIGHT
TITLE 2 CHAIN KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN LIGHT CHAIN KINASE, SMOOTH MUSCLE AND NON-MUSCLE
COMPND 3 ISOZYMES;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: IMMUNOGLOBULIN I-SET DOMAIN;
COMPND 6 SYNONYM: MLCK;
COMPND 7 EC: 2.7.1.117;
COMPND 8 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: MYLK;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050207-03;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS IG FOLD, MLCK, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.HATTA,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CQV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQV 1 VERSN
REVDAT 1 20-NOV-05 2CQV 0
JRNL AUTH R.HATTA,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE EIGHTH IG-LIKE DOMAIN OF HUMAN
JRNL TITL 2 MYOSIN LIGHT CHAIN KINASE
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 2CQV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024522.
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 : 1.64MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL (PH7.0); 100MM
REMARK 210 NACL; 1MM 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 0.9295, 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: SEPECTROMETER_ID 1 FOR 3D_15N-SEPARATED_NOESY;
REMARK 210 SEPECTROMETER_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 ASP A 16 114.35 -38.79
REMARK 500 1 GLU A 23 -175.94 -67.54
REMARK 500 1 ALA A 70 121.95 -36.50
REMARK 500 1 LYS A 85 -31.16 -35.86
REMARK 500 1 LEU A 86 -74.30 -73.55
REMARK 500 1 PRO A 101 -169.84 -69.81
REMARK 500 2 ASP A 16 117.11 -38.97
REMARK 500 2 ALA A 21 112.52 -36.42
REMARK 500 2 ALA A 70 105.56 -37.31
REMARK 500 2 LEU A 86 -75.01 -62.77
REMARK 500 2 PRO A 104 -167.03 -69.81
REMARK 500 2 PRO A 108 96.07 -69.69
REMARK 500 3 SER A 2 42.14 -81.65
REMARK 500 3 ASP A 16 115.25 -34.29
REMARK 500 3 ALA A 21 110.17 -34.15
REMARK 500 3 GLU A 57 77.17 -105.28
REMARK 500 3 ALA A 70 110.51 -36.78
REMARK 500 3 HIS A 74 -39.59 -36.28
REMARK 500 3 LYS A 85 -34.85 -36.78
REMARK 500 3 LEU A 86 -72.64 -72.72
REMARK 500 3 SER A 113 90.13 -65.06
REMARK 500 4 SER A 2 105.33 -51.54
REMARK 500 4 THR A 32 -76.76 -110.36
REMARK 500 4 SER A 59 -178.76 -173.25
REMARK 500 4 ALA A 70 93.38 -37.00
REMARK 500 4 LEU A 86 -75.09 -71.93
REMARK 500 4 PRO A 101 -179.53 -69.78
REMARK 500 4 PRO A 104 -172.75 -69.77
REMARK 500 4 PRO A 111 -177.18 -69.76
REMARK 500 4 SER A 112 -50.28 -126.01
REMARK 500 5 SER A 5 85.31 -66.38
REMARK 500 5 ALA A 21 111.89 -37.12
REMARK 500 5 ALA A 69 52.12 39.42
REMARK 500 5 ALA A 70 136.02 -33.89
REMARK 500 5 LEU A 86 -74.87 -73.76
REMARK 500 5 PRO A 101 -175.13 -69.78
REMARK 500 6 SER A 3 -62.07 -124.31
REMARK 500 6 SER A 5 96.58 -60.14
REMARK 500 6 ALA A 70 106.96 -37.60
REMARK 500 6 LYS A 85 -38.71 -35.63
REMARK 500 6 LEU A 86 -74.23 -69.08
REMARK 500 6 SER A 113 145.89 -38.76
REMARK 500 7 SER A 5 84.24 -64.35
REMARK 500 7 ASP A 16 109.89 -40.00
REMARK 500 7 ALA A 21 113.87 -36.68
REMARK 500 7 ALA A 70 127.31 -33.30
REMARK 500 7 LYS A 85 -36.84 -34.69
REMARK 500 7 LEU A 86 -73.88 -70.07
REMARK 500 7 ALA A 105 148.14 -172.91
REMARK 500 7 SER A 109 145.98 -38.29
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002001434.1 RELATED DB: TARGETDB
DBREF 2CQV A 8 108 UNP Q15746 MYLK_HUMAN 1238 1338
SEQADV 2CQV GLY A 1 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV SER A 2 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV SER A 3 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV GLY A 4 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV SER A 5 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV SER A 6 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV GLY A 7 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV SER A 109 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV GLY A 110 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV PRO A 111 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV SER A 112 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV SER A 113 UNP Q15746 CLONING ARTIFACT
SEQADV 2CQV GLY A 114 UNP Q15746 CLONING ARTIFACT
SEQRES 1 A 114 GLY SER SER GLY SER SER GLY PRO GLN ILE ILE GLN PHE
SEQRES 2 A 114 PRO GLU ASP GLN LYS VAL ARG ALA GLY GLU SER VAL GLU
SEQRES 3 A 114 LEU PHE GLY LYS VAL THR GLY THR GLN PRO ILE THR CYS
SEQRES 4 A 114 THR TRP MET LYS PHE ARG LYS GLN ILE GLN GLU SER GLU
SEQRES 5 A 114 HIS MET LYS VAL GLU ASN SER GLU ASN GLY SER LYS LEU
SEQRES 6 A 114 THR ILE LEU ALA ALA ARG GLN GLU HIS CYS GLY CYS TYR
SEQRES 7 A 114 THR LEU LEU VAL GLU ASN LYS LEU GLY SER ARG GLN ALA
SEQRES 8 A 114 GLN VAL ASN LEU THR VAL VAL ASP LYS PRO ASP PRO PRO
SEQRES 9 A 114 ALA GLY THR PRO SER GLY PRO SER SER GLY
SHEET 1 A 4 GLN A 9 ILE A 10 0
SHEET 2 A 4 VAL A 25 THR A 32 -1 O THR A 32 N GLN A 9
SHEET 3 A 4 GLY A 62 ILE A 67 -1 O LEU A 65 N LEU A 27
SHEET 4 A 4 MET A 54 ASN A 58 -1 N LYS A 55 O THR A 66
SHEET 1 B 4 GLN A 17 ARG A 20 0
SHEET 2 B 4 VAL A 93 VAL A 98 1 O VAL A 98 N VAL A 19
SHEET 3 B 4 GLY A 76 GLU A 83 -1 N TYR A 78 O VAL A 93
SHEET 4 B 4 THR A 38 LYS A 43 -1 N MET A 42 O THR A 79
SHEET 1 C 4 GLN A 17 ARG A 20 0
SHEET 2 C 4 VAL A 93 VAL A 98 1 O VAL A 98 N VAL A 19
SHEET 3 C 4 GLY A 76 GLU A 83 -1 N TYR A 78 O VAL A 93
SHEET 4 C 4 SER A 88 GLN A 90 -1 O ARG A 89 N VAL A 82
CISPEP 1 GLN A 35 PRO A 36 1 -0.08
CISPEP 2 GLN A 35 PRO A 36 2 -0.05
CISPEP 3 GLN A 35 PRO A 36 3 -0.01
CISPEP 4 GLN A 35 PRO A 36 4 0.02
CISPEP 5 GLN A 35 PRO A 36 5 0.04
CISPEP 6 GLN A 35 PRO A 36 6 0.07
CISPEP 7 GLN A 35 PRO A 36 7 -0.05
CISPEP 8 GLN A 35 PRO A 36 8 0.04
CISPEP 9 GLN A 35 PRO A 36 9 -0.07
CISPEP 10 GLN A 35 PRO A 36 10 0.01
CISPEP 11 GLN A 35 PRO A 36 11 -0.02
CISPEP 12 GLN A 35 PRO A 36 12 -0.08
CISPEP 13 GLN A 35 PRO A 36 13 -0.05
CISPEP 14 GLN A 35 PRO A 36 14 -0.04
CISPEP 15 GLN A 35 PRO A 36 15 -0.06
CISPEP 16 GLN A 35 PRO A 36 16 0.02
CISPEP 17 GLN A 35 PRO A 36 17 -0.05
CISPEP 18 GLN A 35 PRO A 36 18 0.02
CISPEP 19 GLN A 35 PRO A 36 19 0.03
CISPEP 20 GLN A 35 PRO A 36 20 -0.13
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