Header list of 1k5o.pdb file
Complete list - 23 20 Bytes
HEADER PROTEIN BINDING 11-OCT-01 1K5O
TITLE CPI-17(35-120) DELETION MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CPI-17;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-86;
COMPND 5 SYNONYM: 17-KDA PKC-POTENTIATED INHIBITORY PROTEIN OF PP1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: PORCINE AORTA;
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_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET30;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET30::CPI(35-120)
KEYWDS PHOSPHORYLATION, PP1-INHIBITOR, MLCP-INHIBITOR, PROTEIN BINDING
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR S.OHKI,M.ETO,E.KARIYA,T.HAYANO,Y.HAYASHI,M.YAZAWA,D.BRAUTIGAN,
AUTHOR 2 M.KAINOSHO
REVDAT 3 23-FEB-22 1K5O 1 REMARK
REVDAT 2 24-FEB-09 1K5O 1 VERSN
REVDAT 1 11-OCT-02 1K5O 0
JRNL AUTH S.OHKI,M.ETO,E.KARIYA,T.HAYANO,Y.HAYASHI,M.YAZAWA,
JRNL AUTH 2 D.BRAUTIGAN,M.KAINOSHO
JRNL TITL SOLUTION NMR STRUCTURE OF THE MYOSIN PHOSPHATASE INHIBITOR
JRNL TITL 2 PROTEIN CPI-17 SHOWS PHOSPHORYLATION-INDUCED CONFORMATIONAL
JRNL TITL 3 CHANGES RESPONSIBLE FOR ACTIVATION
JRNL REF J.MOL.BIOL. V. 314 839 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11734001
JRNL DOI 10.1006/JMBI.2001.5200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1121 NMR-DERIVED DISTANCE AND ANGLE
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1K5O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014591.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 25
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 100MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM 13C/15N LABELED PROTEIN; 1MM
REMARK 210 13C/15N LABELED PROTEIN; 1MM 15N
REMARK 210 LABELED PROTEIN; 1MM UNLABELED
REMARK 210 PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ALA A 1 CA
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 LYS A 64 H THR A 67 1.10
REMARK 500 O VAL A 18 HE1 TRP A 21 1.37
REMARK 500 O LEU A 77 H LEU A 81 1.42
REMARK 500 O ARG A 33 H ASP A 36 1.45
REMARK 500 O ARG A 55 HG12 ILE A 59 1.50
REMARK 500 O LEU A 12 H LEU A 16 1.50
REMARK 500 O LYS A 80 H GLY A 83 1.52
REMARK 500 O ARG A 25 H LEU A 29 1.56
REMARK 500 O TYR A 30 H ARG A 33 1.58
REMARK 500 O VAL A 18 NE1 TRP A 21 2.06
REMARK 500 O LYS A 64 N THR A 67 2.06
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 ARG A 2 -131.69 -57.49
REMARK 500 LYS A 6 -66.49 71.76
REMARK 500 TYR A 7 -174.59 69.96
REMARK 500 ASP A 8 -135.21 -74.42
REMARK 500 ARG A 9 -152.22 -138.49
REMARK 500 ARG A 10 151.95 57.39
REMARK 500 ASP A 23 -39.06 -39.77
REMARK 500 TYR A 30 17.41 -156.76
REMARK 500 ARG A 31 -77.15 -34.47
REMARK 500 ASP A 39 51.90 -110.61
REMARK 500 GLU A 40 57.33 -150.01
REMARK 500 VAL A 41 -166.65 -122.90
REMARK 500 ILE A 43 -38.62 -32.34
REMARK 500 SER A 51 -155.41 -66.68
REMARK 500 GLU A 52 -45.87 -132.31
REMARK 500 LYS A 64 -160.21 71.51
REMARK 500 SER A 65 -46.36 -27.01
REMARK 500 ASN A 68 -157.00 32.89
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 ARG A 2 0.11 SIDE CHAIN
REMARK 500 ARG A 9 0.30 SIDE CHAIN
REMARK 500 ARG A 10 0.17 SIDE CHAIN
REMARK 500 ARG A 14 0.30 SIDE CHAIN
REMARK 500 ARG A 15 0.13 SIDE CHAIN
REMARK 500 ARG A 25 0.28 SIDE CHAIN
REMARK 500 ARG A 31 0.18 SIDE CHAIN
REMARK 500 ARG A 33 0.27 SIDE CHAIN
REMARK 500 ARG A 55 0.11 SIDE CHAIN
REMARK 500 ARG A 57 0.21 SIDE CHAIN
REMARK 500 ARG A 82 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K5O A 1 86 UNP O18734 PP14A_PIG 35 120
SEQRES 1 A 86 ALA ARG VAL THR VAL LYS TYR ASP ARG ARG GLU LEU GLN
SEQRES 2 A 86 ARG ARG LEU ASP VAL GLU LYS TRP ILE ASP GLY ARG LEU
SEQRES 3 A 86 GLU GLU LEU TYR ARG GLY ARG GLU ALA ASP MET PRO ASP
SEQRES 4 A 86 GLU VAL ASN ILE ASP GLU LEU LEU GLU LEU GLU SER GLU
SEQRES 5 A 86 GLU GLU ARG SER ARG LYS ILE GLN GLY LEU LEU LYS SER
SEQRES 6 A 86 CYS THR ASN PRO THR GLU ASN PHE VAL GLN GLU LEU LEU
SEQRES 7 A 86 VAL LYS LEU ARG GLY LEU HIS LYS
HELIX 1 1 GLU A 11 LEU A 16 1 6
HELIX 2 2 LEU A 16 TYR A 30 1 15
HELIX 3 3 ARG A 31 GLU A 34 5 4
HELIX 4 4 VAL A 41 GLU A 48 1 8
HELIX 5 5 GLU A 53 LYS A 64 1 12
HELIX 6 6 SER A 65 THR A 67 5 3
HELIX 7 7 GLU A 71 ARG A 82 1 12
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
Complete list - 23 20 Bytes