Header list of 1tr4.pdb file
Complete list - r 2 2 Bytes
HEADER UNKNOWN FUNCTION 19-JUN-04 1TR4
TITLE SOLUTION STRUCTURE OF HUMAN ONCOGENIC PROTEIN GANKYRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 10;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT P28, GANKYRIN;
COMPND 5 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: PSMD10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GANKYRIN, ONCOPROTEIN, ANKYRIN REPEATS, PROTEIN STRUCTURE, UNKNOWN
KEYWDS 2 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.YUAN,J.LI,A.MAHAJAN,M.J.POI,I.J.BYEON,M.D.TSAI
REVDAT 3 02-MAR-22 1TR4 1 REMARK
REVDAT 2 24-FEB-09 1TR4 1 VERSN
REVDAT 1 16-NOV-04 1TR4 0
JRNL AUTH C.YUAN,J.LI,A.MAHAJAN,M.J.POI,I.J.BYEON,M.D.TSAI
JRNL TITL SOLUTION STRUCTURE OF THE HUMAN ONCOGENIC PROTEIN GANKYRIN
JRNL TITL 2 CONTAINING SEVEN ANKYRIN REPEATS AND ANALYSIS OF ITS
JRNL TITL 3 STRUCTURE--FUNCTION RELATIONSHIP.
JRNL REF BIOCHEMISTRY V. 43 12152 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15379554
JRNL DOI 10.1021/BI049116O
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TR4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022860.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : < 10 MM SALT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : ~0.4 MM GANKYRIN U-15N,13C,70%
REMARK 210 2H; ~0.4 MM GANKYRIN U-15N, 13C;
REMARK 210 ~0.4 MM GANKYRIN U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TROSY-TYPE HNCA, HN(CO)CA,
REMARK 210 HNCACB, CBCA(CO)NH, HNCO; 3D_13C-
REMARK 210 SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; RESIDUAL
REMARK 210 DIPOLAR COUPLING
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, NMRPIPE 1.0,
REMARK 210 NMRVIEW 4.0, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: BACKBONE AMIDE RESIDUAL DIPOLAR COUPLING EXPERIMENT WAS
REMARK 210 PERFORMED IN THE PRESENCE OF FILAMENTOUS PF1 PHAGE
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: 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 ARG A 222 H GLY A 226 1.57
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 VAL A 5 -79.96 -107.26
REMARK 500 1 SER A 6 -49.10 -146.38
REMARK 500 1 LEU A 8 100.54 63.43
REMARK 500 1 LYS A 18 74.01 -100.66
REMARK 500 1 ARG A 35 126.09 -35.51
REMARK 500 1 GLN A 38 -80.16 63.60
REMARK 500 1 HIS A 52 94.35 -37.32
REMARK 500 1 ALA A 72 -33.00 178.50
REMARK 500 1 TRP A 74 -163.26 52.50
REMARK 500 1 ALA A 97 174.46 -46.14
REMARK 500 1 VAL A 99 -37.62 -153.12
REMARK 500 1 ASN A 103 -78.25 -61.82
REMARK 500 1 GLN A 104 -42.58 -150.84
REMARK 500 1 CYS A 107 73.07 -68.61
REMARK 500 1 THR A 108 175.70 -43.45
REMARK 500 1 LYS A 116 -169.22 -110.11
REMARK 500 1 ARG A 118 71.35 -69.97
REMARK 500 1 ASN A 131 103.42 -46.63
REMARK 500 1 LYS A 149 82.68 -167.87
REMARK 500 1 LYS A 162 90.51 69.11
REMARK 500 1 SER A 164 130.89 77.47
REMARK 500 1 THR A 165 46.14 -142.57
REMARK 500 1 ILE A 167 143.61 -30.15
REMARK 500 1 ASN A 173 92.82 175.09
REMARK 500 1 GLU A 183 19.08 57.65
REMARK 500 1 ILE A 200 106.63 -51.76
REMARK 500 1 LYS A 213 37.86 172.23
REMARK 500 1 GLU A 225 34.29 -179.83
REMARK 500 2 VAL A 5 -79.33 -86.69
REMARK 500 2 SER A 6 72.97 172.32
REMARK 500 2 ASN A 7 -147.90 178.71
REMARK 500 2 LYS A 18 65.72 -67.12
REMARK 500 2 ARG A 35 127.65 -29.75
REMARK 500 2 GLN A 38 -84.43 65.01
REMARK 500 2 HIS A 52 96.37 -38.39
REMARK 500 2 VAL A 66 -30.70 -130.71
REMARK 500 2 ASP A 71 2.22 57.48
REMARK 500 2 ALA A 72 -22.60 159.73
REMARK 500 2 TRP A 74 -164.32 51.27
REMARK 500 2 ALA A 97 174.77 -44.56
REMARK 500 2 GLN A 98 -169.46 -76.12
REMARK 500 2 VAL A 99 -41.92 -157.46
REMARK 500 2 CYS A 107 98.89 -68.97
REMARK 500 2 ARG A 118 72.41 -66.24
REMARK 500 2 ASN A 131 101.76 -46.59
REMARK 500 2 ASN A 151 89.49 -163.41
REMARK 500 2 LYS A 162 89.84 71.57
REMARK 500 2 SER A 164 -177.61 -48.81
REMARK 500 2 ASN A 166 12.79 54.07
REMARK 500 2 ILE A 167 142.43 -32.45
REMARK 500
REMARK 500 THIS ENTRY HAS 533 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TR4 A 1 226 UNP O75832 PSD10_HUMAN 1 226
SEQRES 1 A 226 MET GLU GLY CYS VAL SER ASN LEU MET VAL CYS ASN LEU
SEQRES 2 A 226 ALA TYR SER GLY LYS LEU GLU GLU LEU LYS GLU SER ILE
SEQRES 3 A 226 LEU ALA ASP LYS SER LEU ALA THR ARG THR ASP GLN ASP
SEQRES 4 A 226 SER ARG THR ALA LEU HIS TRP ALA CYS SER ALA GLY HIS
SEQRES 5 A 226 THR GLU ILE VAL GLU PHE LEU LEU GLN LEU GLY VAL PRO
SEQRES 6 A 226 VAL ASN ASP LYS ASP ASP ALA GLY TRP SER PRO LEU HIS
SEQRES 7 A 226 ILE ALA ALA SER ALA GLY ARG ASP GLU ILE VAL LYS ALA
SEQRES 8 A 226 LEU LEU GLY LYS GLY ALA GLN VAL ASN ALA VAL ASN GLN
SEQRES 9 A 226 ASN GLY CYS THR PRO LEU HIS TYR ALA ALA SER LYS ASN
SEQRES 10 A 226 ARG HIS GLU ILE ALA VAL MET LEU LEU GLU GLY GLY ALA
SEQRES 11 A 226 ASN PRO ASP ALA LYS ASP HIS TYR GLU ALA THR ALA MET
SEQRES 12 A 226 HIS ARG ALA ALA ALA LYS GLY ASN LEU LYS MET ILE HIS
SEQRES 13 A 226 ILE LEU LEU TYR TYR LYS ALA SER THR ASN ILE GLN ASP
SEQRES 14 A 226 THR GLU GLY ASN THR PRO LEU HIS LEU ALA CYS ASP GLU
SEQRES 15 A 226 GLU ARG VAL GLU GLU ALA LYS LEU LEU VAL SER GLN GLY
SEQRES 16 A 226 ALA SER ILE TYR ILE GLU ASN LYS GLU GLU LYS THR PRO
SEQRES 17 A 226 LEU GLN VAL ALA LYS GLY GLY LEU GLY LEU ILE LEU LYS
SEQRES 18 A 226 ARG MET VAL GLU GLY
HELIX 1 1 LEU A 8 GLY A 17 1 10
HELIX 2 2 LYS A 18 ASP A 29 1 12
HELIX 3 3 LYS A 30 THR A 34 5 5
HELIX 4 4 THR A 42 GLY A 51 1 10
HELIX 5 5 HIS A 52 GLY A 63 1 12
HELIX 6 6 SER A 75 ALA A 83 1 9
HELIX 7 7 ARG A 85 GLY A 94 1 10
HELIX 8 8 THR A 108 LYS A 116 1 9
HELIX 9 9 ARG A 118 ALA A 130 1 13
HELIX 10 10 THR A 141 LYS A 149 1 9
HELIX 11 11 ASN A 151 TYR A 161 1 11
HELIX 12 12 THR A 174 GLU A 182 1 9
HELIX 13 13 ARG A 184 ALA A 196 1 13
HELIX 14 14 THR A 207 GLY A 214 1 8
HELIX 15 15 GLY A 215 GLY A 226 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
MODEL 1
Complete list - r 2 2 Bytes