Header list of 2crp.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 20-MAY-05 2CRP
TITLE SOLUTION STRUCTURE OF THE RGS DOMAIN OF REGULATOR OF G-PROTEIN
TITLE 2 SIGNALLING 5 (RGS 5)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATOR OF G-PROTEIN SIGNALING 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RGS DOMAIN;
COMPND 5 SYNONYM: RGS5;
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 GENE: RGS5;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040322-54;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS RGS DOMAIN, REGULATOR OF G-PROTEIN SIGNALING 5, RGS5, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.P.ZHANG,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CRP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CRP 1 VERSN
REVDAT 1 20-NOV-05 2CRP 0
JRNL AUTH H.P.ZHANG,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RGS DOMAIN OF REGULATOR OF
JRNL TITL 2 G-PROTEIN SIGNALLING 5 (RGS 5)
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 2CRP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024549.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.25MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D-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 5.04,
REMARK 210 KUJIRA 0.9296, 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: SPECTROMETER_ID 1 FOR 3D_15N_SEPARATED_NOESY,
REMARK 210 SPECTROMETER_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 PRO A 8 -178.90 -69.81
REMARK 500 1 PRO A 11 -174.19 -69.84
REMARK 500 1 GLN A 15 170.14 -46.78
REMARK 500 1 LYS A 16 -69.59 -131.64
REMARK 500 1 LYS A 47 -38.89 -39.96
REMARK 500 1 PHE A 50 28.36 45.75
REMARK 500 1 ILE A 85 25.65 -77.01
REMARK 500 1 GLU A 92 105.31 -36.38
REMARK 500 1 PHE A 98 -70.81 -52.15
REMARK 500 1 SER A 111 -68.80 -131.93
REMARK 500 1 LEU A 112 -45.22 -133.40
REMARK 500 1 PHE A 139 -37.73 -32.50
REMARK 500 1 PRO A 147 1.11 -69.88
REMARK 500 2 PRO A 8 -173.24 -69.73
REMARK 500 2 GLU A 9 128.67 -175.00
REMARK 500 2 PRO A 11 -166.39 -69.77
REMARK 500 2 LYS A 16 143.62 -30.29
REMARK 500 2 LYS A 31 -33.61 -38.24
REMARK 500 2 ILE A 85 24.96 -77.58
REMARK 500 2 GLU A 88 34.34 35.15
REMARK 500 2 GLU A 92 100.75 -39.84
REMARK 500 2 VAL A 93 -178.34 -58.66
REMARK 500 2 SER A 111 -71.03 -132.76
REMARK 500 2 LEU A 112 -44.36 -131.35
REMARK 500 2 SER A 148 -30.04 -38.86
REMARK 500 3 PRO A 8 18.09 -69.70
REMARK 500 3 GLU A 9 47.11 -78.37
REMARK 500 3 ILE A 85 25.99 -78.89
REMARK 500 3 GLU A 88 31.62 37.34
REMARK 500 3 ALA A 89 162.59 -49.66
REMARK 500 3 GLU A 92 100.95 -40.60
REMARK 500 3 VAL A 93 -175.02 -58.84
REMARK 500 3 ASP A 96 161.13 -49.42
REMARK 500 3 SER A 111 -70.65 -123.57
REMARK 500 3 LEU A 112 -45.72 -134.83
REMARK 500 3 PHE A 139 -38.38 -37.59
REMARK 500 4 SER A 6 -175.86 -69.72
REMARK 500 4 PRO A 8 7.01 -69.82
REMARK 500 4 GLU A 9 133.15 -27.74
REMARK 500 4 PRO A 11 80.43 -69.76
REMARK 500 4 ALA A 12 -176.96 -172.50
REMARK 500 4 THR A 14 162.93 -44.82
REMARK 500 4 GLN A 15 -68.16 -125.89
REMARK 500 4 ASP A 20 -19.27 -48.18
REMARK 500 4 LYS A 31 -37.29 -37.28
REMARK 500 4 ALA A 74 -62.28 -90.41
REMARK 500 4 ILE A 85 26.82 -78.99
REMARK 500 4 GLU A 92 105.79 -40.91
REMARK 500 4 VAL A 93 -176.33 -61.65
REMARK 500 4 PHE A 98 -70.74 -51.72
REMARK 500
REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000321.1 RELATED DB: TARGETDB
DBREF 2CRP A 8 144 UNP O15539 RGS5_HUMAN 44 180
SEQADV 2CRP GLY A 1 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP SER A 2 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP SER A 3 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP GLY A 4 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP SER A 5 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP SER A 6 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP GLY A 7 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP SER A 145 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP GLY A 146 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP PRO A 147 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP SER A 148 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP SER A 149 UNP O15539 CLONING ARTIFACT
SEQADV 2CRP GLY A 150 UNP O15539 CLONING ARTIFACT
SEQRES 1 A 150 GLY SER SER GLY SER SER GLY PRO GLU LYS PRO ALA LYS
SEQRES 2 A 150 THR GLN LYS THR SER LEU ASP GLU ALA LEU GLN TRP ARG
SEQRES 3 A 150 ASP SER LEU ASP LYS LEU LEU GLN ASN ASN TYR GLY LEU
SEQRES 4 A 150 ALA SER PHE LYS SER PHE LEU LYS SER GLU PHE SER GLU
SEQRES 5 A 150 GLU ASN LEU GLU PHE TRP ILE ALA CYS GLU ASP TYR LYS
SEQRES 6 A 150 LYS ILE LYS SER PRO ALA LYS MET ALA GLU LYS ALA LYS
SEQRES 7 A 150 GLN ILE TYR GLU GLU PHE ILE GLN THR GLU ALA PRO LYS
SEQRES 8 A 150 GLU VAL ASN ILE ASP HIS PHE THR LYS ASP ILE THR MET
SEQRES 9 A 150 LYS ASN LEU VAL GLU PRO SER LEU SER SER PHE ASP MET
SEQRES 10 A 150 ALA GLN LYS ARG ILE HIS ALA LEU MET GLU LYS ASP SER
SEQRES 11 A 150 LEU PRO ARG PHE VAL ARG SER GLU PHE TYR GLN GLU LEU
SEQRES 12 A 150 ILE SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 19 ASP A 27 1 9
HELIX 2 2 LEU A 29 GLN A 34 1 6
HELIX 3 3 ASN A 36 GLU A 49 1 14
HELIX 4 4 GLU A 52 LYS A 65 1 14
HELIX 5 5 LYS A 72 GLU A 83 1 12
HELIX 6 6 HIS A 97 LYS A 105 1 9
HELIX 7 7 ASP A 116 GLN A 119 1 4
HELIX 8 8 LEU A 131 PHE A 134 1 4
HELIX 9 9 GLU A 138 ILE A 144 1 7
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