Header list of 2cqy.pdb file
Complete list - r 9 2 Bytes
HEADER LIGASE 20-MAY-05 2CQY
TITLE SOLUTION STRUCTURE OF B DOMAIN FROM HUMAN PROPIONYL-COA CARBOXYLASE
TITLE 2 ALPHA SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROPIONYL-COA CARBOXYLASE ALPHA CHAIN, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: B DOMAIN;
COMPND 5 SYNONYM: PCCASE ALPHA SUBUNIT, PROPANOYL-COA:CARBON DIOXIDE LIGASE
COMPND 6 ALPHA SUBUNIT;
COMPND 7 EC: 6.4.1.3;
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: PCCA;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040712-08;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS PCCA, B DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.SUETAKE,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CQY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQY 1 VERSN
REVDAT 1 20-NOV-05 2CQY 0
JRNL AUTH T.SUETAKE,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF B DOMAIN FROM HUMAN PROPIONYL-COA
JRNL TITL 2 CARBOXYLASE ALPHA SUBUNIT
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 2CQY 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_1000024525.
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 : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.17MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D10-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 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 0.927, 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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATION, TARGET
REMARK 210 FUNCTION
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 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 GLU A 20 103.03 -44.28
REMARK 500 1 ILE A 102 45.17 -101.48
REMARK 500 1 SER A 103 117.00 -39.95
REMARK 500 2 LEU A 14 109.06 -170.89
REMARK 500 2 GLU A 20 142.72 -173.97
REMARK 500 2 ASP A 28 -34.74 -130.59
REMARK 500 2 MET A 61 -175.63 -57.43
REMARK 500 2 SER A 84 -73.45 -47.76
REMARK 500 2 ARG A 89 109.87 -39.24
REMARK 500 2 PRO A 105 2.89 -69.87
REMARK 500 3 SER A 6 145.24 -170.22
REMARK 500 3 SER A 12 49.16 36.65
REMARK 500 3 LYS A 13 41.42 -95.65
REMARK 500 3 VAL A 21 52.09 34.06
REMARK 500 3 PRO A 25 3.22 -69.72
REMARK 500 3 SER A 84 -65.72 -91.54
REMARK 500 3 PRO A 105 -178.45 -69.75
REMARK 500 3 SER A 107 -62.08 -133.37
REMARK 500 4 LYS A 9 119.23 -167.81
REMARK 500 4 LYS A 13 115.40 -160.47
REMARK 500 4 PRO A 25 2.25 -69.74
REMARK 500 4 LYS A 59 115.52 -39.29
REMARK 500 4 SER A 103 108.46 -43.80
REMARK 500 5 ASP A 8 39.31 35.21
REMARK 500 5 LEU A 15 117.73 -160.76
REMARK 500 5 LYS A 18 141.77 -170.51
REMARK 500 5 ALA A 19 38.73 -95.52
REMARK 500 5 GLU A 20 117.90 -162.48
REMARK 500 5 VAL A 21 35.93 -95.67
REMARK 500 5 PRO A 25 3.01 -69.82
REMARK 500 5 VAL A 30 135.86 -35.26
REMARK 500 5 ALA A 54 42.23 -88.23
REMARK 500 5 PRO A 105 -174.59 -69.68
REMARK 500 6 LYS A 18 52.99 39.54
REMARK 500 6 PHE A 27 107.58 -173.43
REMARK 500 6 MET A 61 -176.47 -57.84
REMARK 500 6 SER A 84 -74.51 -75.67
REMARK 500 6 ARG A 100 98.27 -66.74
REMARK 500 6 SER A 106 45.08 34.35
REMARK 500 7 ILE A 10 29.19 39.01
REMARK 500 7 SER A 12 119.70 -174.66
REMARK 500 7 PHE A 27 134.17 -172.79
REMARK 500 7 TYR A 46 154.08 -48.15
REMARK 500 7 MET A 61 -175.34 -64.93
REMARK 500 7 HIS A 101 43.93 -97.77
REMARK 500 8 SER A 5 146.39 -173.50
REMARK 500 8 ASP A 8 108.57 -173.38
REMARK 500 8 LYS A 13 109.44 -169.51
REMARK 500 8 LYS A 18 43.34 -109.18
REMARK 500 8 PRO A 25 0.48 -69.85
REMARK 500
REMARK 500 THIS ENTRY HAS 151 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002002968.1 RELATED DB: TARGETDB
DBREF 2CQY A 8 102 UNP P05165 PCCA_HUMAN 151 245
SEQADV 2CQY GLY A 1 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY SER A 2 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY SER A 3 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY GLY A 4 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY SER A 5 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY SER A 6 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY GLY A 7 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY SER A 103 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY GLY A 104 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY PRO A 105 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY SER A 106 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY SER A 107 UNP P05165 CLONING ARTIFACT
SEQADV 2CQY GLY A 108 UNP P05165 CLONING ARTIFACT
SEQRES 1 A 108 GLY SER SER GLY SER SER GLY ASP LYS ILE GLU SER LYS
SEQRES 2 A 108 LEU LEU ALA LYS LYS ALA GLU VAL ASN THR ILE PRO GLY
SEQRES 3 A 108 PHE ASP GLY VAL VAL LYS ASP ALA GLU GLU ALA VAL ARG
SEQRES 4 A 108 ILE ALA ARG GLU ILE GLY TYR PRO VAL MET ILE LYS ALA
SEQRES 5 A 108 SER ALA GLY GLY GLY GLY LYS GLY MET ARG ILE ALA TRP
SEQRES 6 A 108 ASP ASP GLU GLU THR ARG ASP GLY PHE ARG LEU SER SER
SEQRES 7 A 108 GLN GLU ALA ALA SER SER PHE GLY ASP ASP ARG LEU LEU
SEQRES 8 A 108 ILE GLU LYS PHE ILE ASP ASN PRO ARG HIS ILE SER GLY
SEQRES 9 A 108 PRO SER SER GLY
HELIX 1 1 ASP A 33 GLY A 45 1 13
HELIX 2 2 ASP A 66 PHE A 85 1 20
SHEET 1 A 3 ARG A 62 ALA A 64 0
SHEET 2 A 3 VAL A 48 ALA A 52 -1 N VAL A 48 O ALA A 64
SHEET 3 A 3 LEU A 90 LYS A 94 -1 O LEU A 91 N LYS A 51
CISPEP 1 TYR A 46 PRO A 47 1 -0.08
CISPEP 2 TYR A 46 PRO A 47 2 -0.06
CISPEP 3 TYR A 46 PRO A 47 3 -0.15
CISPEP 4 TYR A 46 PRO A 47 4 -0.09
CISPEP 5 TYR A 46 PRO A 47 5 -0.01
CISPEP 6 TYR A 46 PRO A 47 6 -0.09
CISPEP 7 TYR A 46 PRO A 47 7 -0.04
CISPEP 8 TYR A 46 PRO A 47 8 -0.03
CISPEP 9 TYR A 46 PRO A 47 9 -0.04
CISPEP 10 TYR A 46 PRO A 47 10 -0.05
CISPEP 11 TYR A 46 PRO A 47 11 -0.02
CISPEP 12 TYR A 46 PRO A 47 12 -0.01
CISPEP 13 TYR A 46 PRO A 47 13 -0.09
CISPEP 14 TYR A 46 PRO A 47 14 -0.13
CISPEP 15 TYR A 46 PRO A 47 15 -0.08
CISPEP 16 TYR A 46 PRO A 47 16 -0.06
CISPEP 17 TYR A 46 PRO A 47 17 -0.04
CISPEP 18 TYR A 46 PRO A 47 18 -0.15
CISPEP 19 TYR A 46 PRO A 47 19 -0.06
CISPEP 20 TYR A 46 PRO A 47 20 -0.03
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