Header list of 1pd6.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN 19-MAY-03 1PD6
TITLE THE NMR STRUCTURE OF DOMAIN C2 OF HUMAN CARDIAC MYOSIN BINDING PROTEIN
TITLE 2 C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-BINDING PROTEIN C, CARDIAC-TYPE, DOMAIN C2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN C2;
COMPND 5 SYNONYM: CARDIAC MYOSIN-BINDING PROTEIN C; CARDIAC MYBP-C; PROTEIN C,
COMPND 6 CARDIAC;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: HEART;
SOURCE 6 TISSUE: MUSCLE;
SOURCE 7 GENE: MYBPC3;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21*;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET-8A
KEYWDS IG DOMAIN, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 28
AUTHOR A.ABABOU,M.GAUTEL,M.PFUHL
REVDAT 3 23-FEB-22 1PD6 1 REMARK SEQADV
REVDAT 2 22-JUL-08 1PD6 1 VERSN JRNL
REVDAT 1 03-AUG-04 1PD6 0
JRNL AUTH A.ABABOU,M.GAUTEL,M.PFUHL
JRNL TITL DISSECTING THE N-TERMINAL MYOSIN BINDING SITE OF HUMAN
JRNL TITL 2 CARDIAC MYOSIN-BINDING PROTEIN C. STRUCTURE AND MYOSIN
JRNL TITL 3 BINDING OF DOMAIN C2
JRNL REF J.BIOL.CHEM. V. 282 9204 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17192269
JRNL DOI 10.1074/JBC.M610899200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ANSIG 3.3, ARIA 1.1
REMARK 3 AUTHORS : KRAULIS, J. (ANSIG), LINGE, J., O'DONOGHUE, S.,
REMARK 3 NILGES, M. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PD6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019245.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 7.0; 7.0; 7.0
REMARK 210 IONIC STRENGTH : 0.1; 0.1; 7.0
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.75MM C2; 15N; 20MM PHOSPHATE
REMARK 210 BUFFER; 90% H2O, 10% D2O; 0.75MM
REMARK 210 C2; 15N, 13C; 20MM PHOSPHATE
REMARK 210 BUFFER; 90% H2O, 10% D2O; 0.75MM
REMARK 210 C2; 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 : ARIA 1.1, NMRPIPE 290302, AZARA
REMARK 210 2.6
REMARK 210 METHOD USED : WE HAVE USED ARIA PROTOCOLS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 28
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: FURTHER NMR EXPERIMENTS COULD BE FOUND IN THE BMRB
REMARK 210 ACCESSION NUMBER 5591
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 1-28
REMARK 465 RES C SSSEQI
REMARK 465 MET A 198
REMARK 465 HIS A 199
REMARK 465 HIS A 200
REMARK 465 HIS A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 SER A 205
REMARK 465 SER A 206
REMARK 465 MET A 207
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 HB3 LEU A 247 HE21 GLN A 285 0.96
REMARK 500 HB2 LEU A 233 HB3 LEU A 271 1.29
REMARK 500 HD2 LYS A 227 HA GLU A 301 1.34
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 4 TYR A 223 CZ TYR A 223 CE2 -0.081
REMARK 500 11 TYR A 223 CE1 TYR A 223 CZ 0.108
REMARK 500 11 TYR A 223 CZ TYR A 223 CE2 -0.103
REMARK 500 13 TYR A 223 CZ TYR A 223 CE2 -0.080
REMARK 500 16 TYR A 260 CZ TYR A 260 CE2 -0.080
REMARK 500 22 TYR A 223 CE1 TYR A 223 CZ 0.081
REMARK 500 22 TYR A 223 CZ TYR A 223 CE2 -0.092
REMARK 500 23 TYR A 223 CZ TYR A 223 CE2 -0.079
REMARK 500 24 TYR A 223 CE1 TYR A 223 CZ 0.095
REMARK 500 24 TYR A 223 CZ TYR A 223 CE2 -0.092
REMARK 500 25 TYR A 223 CE1 TYR A 223 CZ 0.089
REMARK 500 25 TYR A 223 CZ TYR A 223 CE2 -0.097
REMARK 500 26 TYR A 223 CZ TYR A 223 CE2 -0.079
REMARK 500 26 TYR A 284 CE1 TYR A 284 CZ -0.082
REMARK 500 28 TYR A 223 CE1 TYR A 223 CZ 0.103
REMARK 500 28 TYR A 223 CZ TYR A 223 CE2 -0.107
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 SER A 212 -40.45 177.04
REMARK 500 1 THR A 213 155.70 -48.17
REMARK 500 1 ALA A 214 28.28 -71.15
REMARK 500 1 PRO A 221 36.27 -66.39
REMARK 500 1 ALA A 222 84.34 -157.53
REMARK 500 1 LYS A 230 107.63 71.12
REMARK 500 1 HIS A 240 -57.79 78.94
REMARK 500 1 ASN A 249 106.60 -47.31
REMARK 500 1 GLN A 254 -121.67 -83.07
REMARK 500 1 SER A 258 -27.02 -156.12
REMARK 500 1 ALA A 267 -39.34 75.97
REMARK 500 1 SER A 277 -129.27 -148.34
REMARK 500 1 ALA A 279 -46.30 -157.51
REMARK 500 1 ALA A 282 -112.32 -171.17
REMARK 500 2 LYS A 210 153.57 175.80
REMARK 500 2 SER A 212 -115.19 -157.40
REMARK 500 2 THR A 213 -168.06 53.45
REMARK 500 2 PRO A 221 40.88 -66.35
REMARK 500 2 ALA A 222 81.42 -163.18
REMARK 500 2 LYS A 230 108.94 69.49
REMARK 500 2 HIS A 240 -34.50 74.67
REMARK 500 2 ASP A 241 69.33 -158.02
REMARK 500 2 SER A 256 -151.83 -150.82
REMARK 500 2 SER A 258 -65.50 -160.11
REMARK 500 2 SER A 277 -133.93 -78.23
REMARK 500 2 ALA A 279 -44.50 -165.85
REMARK 500 2 ASP A 281 116.91 -15.39
REMARK 500 2 ALA A 282 -112.14 -177.14
REMARK 500 3 LYS A 210 -107.16 177.73
REMARK 500 3 SER A 212 -131.32 -176.88
REMARK 500 3 PRO A 221 35.68 -63.93
REMARK 500 3 ALA A 222 87.31 -160.10
REMARK 500 3 HIS A 229 -71.48 -86.87
REMARK 500 3 LYS A 230 113.14 158.48
REMARK 500 3 HIS A 240 -55.74 76.51
REMARK 500 3 ASN A 249 108.03 -47.03
REMARK 500 3 GLN A 254 -110.50 -83.11
REMARK 500 3 CYS A 276 62.80 -154.45
REMARK 500 3 SER A 277 -129.00 -89.51
REMARK 500 3 ALA A 279 -43.92 -164.54
REMARK 500 3 ALA A 282 -118.34 -171.61
REMARK 500 4 LYS A 210 -112.61 -150.77
REMARK 500 4 SER A 212 -125.04 -163.88
REMARK 500 4 THR A 213 -173.80 52.86
REMARK 500 4 PRO A 221 37.10 -66.45
REMARK 500 4 ALA A 222 85.42 -157.19
REMARK 500 4 LYS A 230 107.53 69.76
REMARK 500 4 HIS A 240 -62.77 75.38
REMARK 500 4 ASP A 241 57.00 -108.12
REMARK 500 4 SER A 256 -159.85 -151.55
REMARK 500
REMARK 500 THIS ENTRY HAS 408 RAMACHANDRAN OUTLIERS.
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 223 0.05 SIDE CHAIN
REMARK 500 11 TYR A 223 0.06 SIDE CHAIN
REMARK 500 23 TYR A 223 0.06 SIDE CHAIN
REMARK 500 24 TYR A 223 0.06 SIDE CHAIN
REMARK 500 25 TYR A 223 0.05 SIDE CHAIN
REMARK 500 28 TYR A 260 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 4 SER A 226 10.02
REMARK 500 5 SER A 226 10.08
REMARK 500 6 SER A 226 10.70
REMARK 500 7 SER A 226 10.21
REMARK 500 10 SER A 226 10.26
REMARK 500 12 SER A 226 10.86
REMARK 500 15 VAL A 225 -10.00
REMARK 500 15 SER A 226 10.45
REMARK 500 20 SER A 212 11.36
REMARK 500 20 SER A 226 10.21
REMARK 500 20 LYS A 245 10.30
REMARK 500 20 TRP A 246 11.36
REMARK 500 21 SER A 226 10.52
REMARK 500 22 TRP A 246 10.23
REMARK 500 24 CYS A 276 10.44
REMARK 500 25 SER A 226 10.80
REMARK 500 27 SER A 226 10.19
REMARK 500 27 TRP A 246 10.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GXE RELATED DB: PDB
REMARK 900 THE FIRST STRUCTURE OF A DOMAIN OF MYOSIN BINDING PROTEIN C
DBREF 1PD6 A 208 301 UNP Q14896 MYPC3_HUMAN 358 451
SEQADV 1PD6 MET A 198 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 HIS A 199 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 HIS A 200 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 HIS A 201 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 HIS A 202 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 HIS A 203 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 HIS A 204 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 SER A 205 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 SER A 206 UNP Q14896 EXPRESSION TAG
SEQADV 1PD6 MET A 207 UNP Q14896 EXPRESSION TAG
SEQRES 1 A 104 MET HIS HIS HIS HIS HIS HIS SER SER MET ASP GLU LYS
SEQRES 2 A 104 LYS SER THR ALA PHE GLN LYS LYS LEU GLU PRO ALA TYR
SEQRES 3 A 104 GLN VAL SER LYS GLY HIS LYS ILE ARG LEU THR VAL GLU
SEQRES 4 A 104 LEU ALA ASP HIS ASP ALA GLU VAL LYS TRP LEU LYS ASN
SEQRES 5 A 104 GLY GLN GLU ILE GLN MET SER GLY SER LYS TYR ILE PHE
SEQRES 6 A 104 GLU SER ILE GLY ALA LYS ARG THR LEU THR ILE SER GLN
SEQRES 7 A 104 CYS SER LEU ALA ASP ASP ALA ALA TYR GLN CYS VAL VAL
SEQRES 8 A 104 GLY GLY GLU LYS CYS SER THR GLU LEU PHE VAL LYS GLU
SHEET 1 A 4 LYS A 217 LYS A 218 0
SHEET 2 A 4 ILE A 231 GLU A 236 -1 O GLU A 236 N LYS A 217
SHEET 3 A 4 LYS A 268 ILE A 273 -1 O ILE A 273 N ILE A 231
SHEET 4 A 4 ILE A 261 ILE A 265 -1 N ILE A 261 O THR A 272
SHEET 1 B 5 ALA A 222 SER A 226 0
SHEET 2 B 5 GLU A 296 LYS A 300 1 O PHE A 298 N TYR A 223
SHEET 3 B 5 ALA A 282 VAL A 288 -1 N ALA A 282 O LEU A 297
SHEET 4 B 5 LYS A 245 LYS A 248 -1 N LEU A 247 O GLN A 285
SHEET 5 B 5 GLU A 252 ILE A 253 -1 O ILE A 253 N TRP A 246
SHEET 1 C 4 ALA A 222 SER A 226 0
SHEET 2 C 4 GLU A 296 LYS A 300 1 O PHE A 298 N TYR A 223
SHEET 3 C 4 ALA A 282 VAL A 288 -1 N ALA A 282 O LEU A 297
SHEET 4 C 4 GLU A 291 CYS A 293 -1 O CYS A 293 N CYS A 286
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 - b 23 2 Bytes