HEADER STRUCTURAL PROTEIN 30-AUG-05 2AVG
TITLE NMR STRUCTURE OF CC1 DOMAIN FROM HUMAN CARDIAC MYOSIN BINDING PROTEIN
TITLE 2 C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-BINDING PROTEIN C, CARDIAC-TYPE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CC1 DOMAIN;
COMPND 5 SYNONYM: CARDIAC MYBP-C, C-PROTEIN, CARDIAC MUSCLE 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21*;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-8A
KEYWDS HUMAN CARDIAC MYBP-C, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR A.ABABOU,M.GAUTEL,M.PFUHL
REVDAT 6 14-JUN-23 2AVG 1 REMARK
REVDAT 5 26-FEB-20 2AVG 1 REMARK SEQADV
REVDAT 4 09-JUN-09 2AVG 1 REVDAT
REVDAT 3 24-FEB-09 2AVG 1 VERSN
REVDAT 2 13-JAN-09 2AVG 1 JRNL
REVDAT 1 05-SEP-06 2AVG 0
JRNL AUTH A.ABABOU,E.ROSTKOVA,S.MISTRY,C.LE MASURIER,M.GAUTEL,M.PFUHL
JRNL TITL MYOSIN BINDING PROTEIN C POSITIONED TO PLAY A KEY ROLE IN
JRNL TITL 2 REGULATION OF MUSCLE CONTRACTION: STRUCTURE AND INTERACTIONS
JRNL TITL 3 OF DOMAIN C1.
JRNL REF J.MOL.BIOL. V. 384 615 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18926831
JRNL DOI 10.1016/J.JMB.2008.09.065
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 290302, ARIA 1.2
REMARK 3 AUTHORS : DELAGLIO F. (NMRPIPE), LINGE J. & NILGES M. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AVG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034360.
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 : 0.1M
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM CC1 U-15N; 20MM PHOSPHATE
REMARK 210 BUFFER; 90% H2O, 10% D2O; 0.8MM
REMARK 210 CC1 U-15N, 13C; 20MM PHOSPHATE
REMARK 210 BUFFER; 90% H2O, 10% D2O; 0.8MM
REMARK 210 CC1 U-15N, 13C; 20MM PHOSPHATE
REMARK 210 BUFFER; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; UNITYINOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, ARIA 1.2, AZARA 2.6
REMARK 210 METHOD USED : SIMULATED ANNEALING USING ARIA
REMARK 210 PROGRAM
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATION > 0.5 A
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 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 1-29
REMARK 465 RES C SSSEQI
REMARK 465 MET A -10
REMARK 465 HIS 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 SER A -3
REMARK 465 SER A -2
REMARK 465 MET 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 HZ3 TRP A 41 HZ PHE A 102 1.14
REMARK 500 HB3 TRP A 41 HD12 LEU A 49 1.29
REMARK 500 HB3 GLU A 15 HE2 HIS A 107 1.31
REMARK 500 HA2 GLY A 44 HA2 GLY A 85 1.33
REMARK 500 HD23 LEU A 49 HD23 LEU A 57 1.34
REMARK 500 OD2 ASP A 2 HZ2 LYS A 94 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 5 PHE A 83 CE1 PHE A 83 CZ 0.157
REMARK 500 5 PHE A 83 CZ PHE A 83 CE2 -0.137
REMARK 500 6 PHE A 83 CE1 PHE A 83 CZ 0.128
REMARK 500 6 PHE A 83 CZ PHE A 83 CE2 -0.114
REMARK 500 11 PHE A 83 CE1 PHE A 83 CZ 0.148
REMARK 500 11 PHE A 83 CZ PHE A 83 CE2 -0.133
REMARK 500 18 PHE A 83 CE1 PHE A 83 CZ 0.122
REMARK 500 20 TYR A 70 CE1 TYR A 70 CZ 0.087
REMARK 500 20 TYR A 70 CZ TYR A 70 CE2 -0.091
REMARK 500 21 TYR A 87 CE1 TYR A 87 CZ 0.083
REMARK 500 21 TYR A 87 CZ TYR A 87 CE2 -0.100
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 14 THR A 84 CA - CB - CG2 ANGL. DEV. = -10.4 DEGREES
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 ASP A 13 -146.22 -68.23
REMARK 500 1 ALA A 31 -176.87 -50.68
REMARK 500 1 LYS A 45 -8.68 -42.62
REMARK 500 1 TRP A 46 -6.31 -162.09
REMARK 500 1 VAL A 53 94.02 -36.43
REMARK 500 1 ASP A 78 73.50 50.68
REMARK 500 1 THR A 84 90.63 -17.97
REMARK 500 1 LYS A 94 -77.32 23.20
REMARK 500 1 ASP A 95 -3.78 -144.17
REMARK 500 2 PRO A 3 86.91 -68.84
REMARK 500 2 ASP A 13 -150.48 -67.94
REMARK 500 2 ALA A 31 -174.22 59.96
REMARK 500 2 LYS A 45 -11.04 -45.23
REMARK 500 2 TRP A 46 -2.87 -164.18
REMARK 500 2 VAL A 53 96.05 -37.54
REMARK 500 2 ASP A 78 75.73 38.45
REMARK 500 2 THR A 84 98.51 -46.28
REMARK 500 2 LYS A 94 -73.12 18.61
REMARK 500 2 ASP A 95 1.23 -151.81
REMARK 500 2 ALA A 109 18.10 53.51
REMARK 500 3 PRO A 3 84.41 -67.37
REMARK 500 3 ASP A 13 -141.26 -71.42
REMARK 500 3 ALA A 31 -167.06 49.23
REMARK 500 3 TRP A 46 -13.59 157.85
REMARK 500 3 VAL A 53 95.78 -22.57
REMARK 500 3 ASP A 78 101.47 67.65
REMARK 500 3 LYS A 94 -60.48 -3.50
REMARK 500 3 ASP A 95 5.19 -163.93
REMARK 500 3 ALA A 109 -78.23 -88.26
REMARK 500 4 PRO A 3 83.58 -60.95
REMARK 500 4 ASP A 13 -147.19 -65.62
REMARK 500 4 ALA A 31 -172.26 56.10
REMARK 500 4 LYS A 45 -9.07 -44.37
REMARK 500 4 TRP A 46 -3.30 -167.67
REMARK 500 4 VAL A 53 95.09 -32.34
REMARK 500 4 THR A 84 94.25 -28.97
REMARK 500 4 LYS A 94 -73.52 17.92
REMARK 500 4 ASP A 95 1.97 -150.74
REMARK 500 4 GLU A 108 -74.30 -63.45
REMARK 500 5 PRO A 3 45.95 -69.03
REMARK 500 5 ASP A 13 -144.58 -68.33
REMARK 500 5 VAL A 18 107.45 -57.93
REMARK 500 5 ALA A 31 -143.98 47.09
REMARK 500 5 LEU A 33 147.53 171.00
REMARK 500 5 LYS A 45 -1.73 -45.47
REMARK 500 5 TRP A 46 -10.02 -166.03
REMARK 500 5 LYS A 52 -67.93 -94.11
REMARK 500 5 VAL A 53 93.20 12.80
REMARK 500 5 ASP A 78 78.24 39.38
REMARK 500 5 THR A 84 79.77 22.67
REMARK 500
REMARK 500 THIS ENTRY HAS 337 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 44 LYS A 45 3 138.95
REMARK 500 GLY A 44 LYS A 45 9 123.06
REMARK 500 GLY A 44 LYS A 45 13 137.30
REMARK 500 GLY A 85 GLY A 86 15 149.86
REMARK 500 GLY A 44 LYS A 45 16 134.41
REMARK 500 GLY A 44 LYS A 45 17 137.38
REMARK 500 GLY A 44 LYS A 45 22 139.55
REMARK 500 GLY A 44 LYS A 45 23 135.22
REMARK 500 GLY A 44 LYS A 45 27 132.16
REMARK 500 GLY A 44 LYS A 45 28 135.32
REMARK 500 GLY A 44 LYS A 45 29 -140.24
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 2 TYR A 70 0.06 SIDE CHAIN
REMARK 500 13 TYR A 63 0.05 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 2 GLY A 44 10.16
REMARK 500 4 GLY A 44 10.99
REMARK 500 10 GLY A 44 10.51
REMARK 500 21 GLY A 44 10.27
REMARK 500 26 GLY A 44 10.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6015 RELATED DB: BMRB
DBREF 2AVG A 1 110 UNP Q14896 MYPC3_HUMAN 151 260
SEQADV 2AVG MET A -10 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG HIS A -9 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG HIS A -8 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG HIS A -7 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG HIS A -6 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG HIS A -5 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG HIS A -4 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG SER A -3 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG SER A -2 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG MET A -1 UNP Q14896 EXPRESSION TAG
SEQADV 2AVG GLY A 86 UNP Q14896 SER 236 SEE REMARK 999
SEQRES 1 A 120 MET HIS HIS HIS HIS HIS HIS SER SER MET ASP ASP PRO
SEQRES 2 A 120 ILE GLY LEU PHE VAL MET ARG PRO GLN ASP GLY GLU VAL
SEQRES 3 A 120 THR VAL GLY GLY SER ILE THR PHE SER ALA ARG VAL ALA
SEQRES 4 A 120 GLY ALA SER LEU LEU LYS PRO PRO VAL VAL LYS TRP PHE
SEQRES 5 A 120 LYS GLY LYS TRP VAL ASP LEU SER SER LYS VAL GLY GLN
SEQRES 6 A 120 HIS LEU GLN LEU HIS ASP SER TYR ASP ARG ALA SER LYS
SEQRES 7 A 120 VAL TYR LEU PHE GLU LEU HIS ILE THR ASP ALA GLN PRO
SEQRES 8 A 120 ALA PHE THR GLY GLY TYR ARG CYS GLU VAL SER THR LYS
SEQRES 9 A 120 ASP LYS PHE ASP CYS SER ASN PHE ASN LEU THR VAL HIS
SEQRES 10 A 120 GLU ALA MET
SHEET 1 A 4 PHE A 7 MET A 9 0
SHEET 2 A 4 SER A 21 ALA A 29 -1 O ARG A 27 N MET A 9
SHEET 3 A 4 VAL A 69 THR A 77 -1 O TYR A 70 N VAL A 28
SHEET 4 A 4 LEU A 57 ASP A 64 -1 N ASP A 64 O VAL A 69
SHEET 1 B 4 GLY A 14 THR A 17 0
SHEET 2 B 4 LYS A 96 HIS A 107 1 O HIS A 107 N VAL A 16
SHEET 3 B 4 GLY A 85 THR A 93 -1 N CYS A 89 O SER A 100
SHEET 4 B 4 VAL A 38 PHE A 42 -1 N VAL A 38 O SER A 92
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
(ATOM LINES ARE NOT SHOWN.)
END