Header list of 1xwn.pdb file
Complete list - r 2 2 Bytes
HEADER ISOMERASE 01-NOV-04 1XWN
TITLE SOLUTION STRUCTURE OF CYCLOPHILIN LIKE 1(PPIL1) AND INSIGHTS INTO ITS
TITLE 2 INTERACTION WITH SKIP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE LIKE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PPIASE, ROTAMASE, CGI-124, UNQ2425/PRO4984;
COMPND 5 EC: 5.2.1.8;
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: PPIL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)
KEYWDS BETA BARREL, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.XU,Y.XU,Y.TANG,J.WU,Y.SHI,Q.HUANG,Q.ZHANG
REVDAT 4 02-MAR-22 1XWN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1XWN 1 VERSN
REVDAT 2 13-JUN-06 1XWN 1 JRNL
REVDAT 1 18-OCT-05 1XWN 0
JRNL AUTH C.XU,J.ZHANG,X.HUANG,J.SUN,Y.XU,Y.TANG,J.WU,Y.SHI,Q.HUANG,
JRNL AUTH 2 Q.ZHANG
JRNL TITL SOLUTION STRUCTURE OF HUMAN PEPTIDYL PROLYL ISOMERASE LIKE
JRNL TITL 2 PROTEIN 1 AND INSIGHTS INTO ITS INTERACTION WITH SKIP
JRNL REF J.BIOL.CHEM. V. 281 15900 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16595688
JRNL DOI 10.1074/JBC.M511155200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CNS 1.1
REMARK 3 AUTHORS : DELAGIO (NMRPIPE),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XWN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030851.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50MM NACL, 20MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM PPIL1, U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA, 50MM NACL,
REMARK 210 90% H2O, 10% D2O; 0.5MM PPIL1, U-
REMARK 210 15N,13C; 20MM PHOSPHATE BUFFER
REMARK 210 NA, 50MM NACL, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.110
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 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 LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 167
REMARK 465 GLU A 168
REMARK 465 HIS A 169
REMARK 465 HIS A 170
REMARK 465 HIS A 171
REMARK 465 HIS A 172
REMARK 465 HIS A 173
REMARK 465 HIS A 174
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 ALA A 2 92.53 59.72
REMARK 500 1 TRP A 9 -60.64 -99.08
REMARK 500 1 GLN A 10 109.21 63.10
REMARK 500 1 LYS A 30 -66.51 -100.42
REMARK 500 1 PRO A 33 -35.63 -39.48
REMARK 500 1 PHE A 60 -84.61 -157.73
REMARK 500 1 ASP A 66 -58.54 -174.87
REMARK 500 1 THR A 70 22.24 -156.31
REMARK 500 1 GLU A 85 40.58 -94.54
REMARK 500 1 PRO A 88 101.61 -53.92
REMARK 500 1 ASP A 89 -46.02 -172.28
REMARK 500 1 PHE A 92 61.34 -112.99
REMARK 500 1 ALA A 103 -51.91 -121.83
REMARK 500 1 ASP A 123 81.21 -61.82
REMARK 500 1 PHE A 129 -40.36 -177.45
REMARK 500 1 GLN A 150 -72.14 -155.36
REMARK 500 1 ASP A 151 41.83 -172.84
REMARK 500 1 ASP A 155 -167.11 -79.88
REMARK 500 2 PRO A 5 107.58 -53.63
REMARK 500 2 ASP A 7 152.94 69.47
REMARK 500 2 TRP A 9 118.48 -166.36
REMARK 500 2 PRO A 11 104.30 -47.86
REMARK 500 2 LYS A 30 -69.36 -100.41
REMARK 500 2 PHE A 53 179.09 59.86
REMARK 500 2 HIS A 54 -70.96 -145.11
REMARK 500 2 PHE A 60 -88.49 -160.41
REMARK 500 2 ASP A 66 -64.71 -160.60
REMARK 500 2 ARG A 72 -52.23 -165.21
REMARK 500 2 GLN A 81 135.63 70.80
REMARK 500 2 GLU A 83 -179.62 -67.83
REMARK 500 2 HIS A 87 -62.39 -171.99
REMARK 500 2 THR A 107 80.50 -152.19
REMARK 500 2 SER A 110 25.43 -149.44
REMARK 500 2 ASP A 123 79.52 -68.76
REMARK 500 2 PHE A 129 -42.90 -170.46
REMARK 500 2 SER A 149 30.28 -95.21
REMARK 500 2 GLN A 150 32.07 -152.65
REMARK 500 2 ALA A 162 87.31 -156.53
REMARK 500 3 ALA A 3 62.77 -116.63
REMARK 500 3 ILE A 4 87.85 -173.66
REMARK 500 3 TRP A 9 -51.29 -129.89
REMARK 500 3 PRO A 11 109.55 -55.66
REMARK 500 3 LYS A 30 -61.87 -100.32
REMARK 500 3 PRO A 33 -38.15 -38.96
REMARK 500 3 PHE A 60 -83.30 -152.30
REMARK 500 3 ASP A 66 73.53 -114.85
REMARK 500 3 ARG A 72 -46.42 -177.76
REMARK 500 3 HIS A 87 86.70 -162.79
REMARK 500 3 PRO A 88 100.59 -54.99
REMARK 500 3 ASP A 89 -44.83 -165.71
REMARK 500
REMARK 500 THIS ENTRY HAS 374 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6310 RELATED DB: BMRB
DBREF 1XWN A 1 166 UNP Q9Y3C6 PPIL1_HUMAN 1 166
SEQADV 1XWN LEU A 167 UNP Q9Y3C6 EXPRESSION TAG
SEQADV 1XWN GLU A 168 UNP Q9Y3C6 EXPRESSION TAG
SEQADV 1XWN HIS A 169 UNP Q9Y3C6 EXPRESSION TAG
SEQADV 1XWN HIS A 170 UNP Q9Y3C6 EXPRESSION TAG
SEQADV 1XWN HIS A 171 UNP Q9Y3C6 EXPRESSION TAG
SEQADV 1XWN HIS A 172 UNP Q9Y3C6 EXPRESSION TAG
SEQADV 1XWN HIS A 173 UNP Q9Y3C6 EXPRESSION TAG
SEQADV 1XWN HIS A 174 UNP Q9Y3C6 EXPRESSION TAG
SEQRES 1 A 174 MET ALA ALA ILE PRO PRO ASP SER TRP GLN PRO PRO ASN
SEQRES 2 A 174 VAL TYR LEU GLU THR SER MET GLY ILE ILE VAL LEU GLU
SEQRES 3 A 174 LEU TYR TRP LYS HIS ALA PRO LYS THR CYS LYS ASN PHE
SEQRES 4 A 174 ALA GLU LEU ALA ARG ARG GLY TYR TYR ASN GLY THR LYS
SEQRES 5 A 174 PHE HIS ARG ILE ILE LYS ASP PHE MET ILE GLN GLY GLY
SEQRES 6 A 174 ASP PRO THR GLY THR GLY ARG GLY GLY ALA SER ILE TYR
SEQRES 7 A 174 GLY LYS GLN PHE GLU ASP GLU LEU HIS PRO ASP LEU LYS
SEQRES 8 A 174 PHE THR GLY ALA GLY ILE LEU ALA MET ALA ASN ALA GLY
SEQRES 9 A 174 PRO ASP THR ASN GLY SER GLN PHE PHE VAL THR LEU ALA
SEQRES 10 A 174 PRO THR GLN TRP LEU ASP GLY LYS HIS THR ILE PHE GLY
SEQRES 11 A 174 ARG VAL CYS GLN GLY ILE GLY MET VAL ASN ARG VAL GLY
SEQRES 12 A 174 MET VAL GLU THR ASN SER GLN ASP ARG PRO VAL ASP ASP
SEQRES 13 A 174 VAL LYS ILE ILE LYS ALA TYR PRO SER GLY LEU GLU HIS
SEQRES 14 A 174 HIS HIS HIS HIS HIS
HELIX 1 1 ALA A 32 ARG A 45 1 14
HELIX 2 2 GLY A 135 VAL A 145 1 11
SHEET 1 A 8 PHE A 53 ILE A 57 0
SHEET 2 A 8 MET A 61 GLY A 64 -1 O MET A 61 N ILE A 57
SHEET 3 A 8 THR A 107 THR A 115 -1 O PHE A 112 N GLY A 64
SHEET 4 A 8 ILE A 97 GLY A 104 -1 N GLY A 104 O THR A 107
SHEET 5 A 8 THR A 127 ARG A 131 -1 O GLY A 130 N LEU A 98
SHEET 6 A 8 ILE A 22 LEU A 27 -1 N GLU A 26 O ARG A 131
SHEET 7 A 8 ASN A 13 THR A 18 -1 N VAL A 14 O LEU A 25
SHEET 8 A 8 ILE A 159 PRO A 164 -1 O TYR A 163 N TYR A 15
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