HEADER ISOMERASE 20-JAN-15 2RUR
TITLE SOLUTION STRUCTURE OF HUMAN PIN1 PPIASE C113S MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 51-163;
COMPND 5 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE PIN1, PPIASE PIN1,
COMPND 6 ROTAMASE PIN1;
COMPND 7 EC: 5.2.1.8;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PIN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS CYS-113 MUTATION, HUMAN PIN1 PPIASE, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR W.JING,N.TOCHIO,S.TATE
REVDAT 2 14-JUN-23 2RUR 1 REMARK SEQADV
REVDAT 1 06-JAN-16 2RUR 0
JRNL AUTH J.WANG,N.TOCHIO,R.KAWASAKI,Y.TAMARI,N.XU,J.UEWAKI,
JRNL AUTH 2 N.UTSUNOMIYA-TATE,S.TATE
JRNL TITL ALLOSTERIC BREAKAGE OF THE HYDROGEN BOND WITHIN THE
JRNL TITL 2 DUAL-HISTIDINE MOTIF IN THE ACTIVE SITE OF HUMAN PIN1 PPIASE
JRNL REF BIOCHEMISTRY V. 54 5242 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 26226559
JRNL DOI 10.1021/ACS.BIOCHEM.5B00606
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN, X-PLOR NIH
REMARK 3 AUTHORS : BRUKER BIOSPIN (TOPSPIN), SCHWIETERS, KUSZEWSKI,
REMARK 3 TJANDRA AND CLORE (X-PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2RUR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000150291.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : 150
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 100 MM SODIUM SULFATE-1, 50 MM
REMARK 210 SODIUM PHOSPHATE-2, 6 % [U-2H]
REMARK 210 D2O-3, 94 % H2O-4, 5 MM EDTA-5,
REMARK 210 1 MM DTT-6, 0.03 % NAN3-7, 94%
REMARK 210 H2O/6% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-13C NOESY; 3D 1H-15N NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, MAGRO, NMRVIEW, CYANA,
REMARK 210 SPARKY, X-PLOR NIH
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 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: 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
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 ARG A 28 -32.03 -134.35
REMARK 500 2 PRO A 6 105.32 -54.80
REMARK 500 2 GLN A 20 38.22 -84.03
REMARK 500 2 GLN A 63 -57.51 -133.77
REMARK 500 3 GLU A 5 153.45 73.00
REMARK 500 3 PRO A 24 33.69 -80.01
REMARK 500 3 GLN A 63 -58.68 -126.01
REMARK 500 3 PHE A 64 38.40 -93.94
REMARK 500 3 ARG A 81 -82.38 64.48
REMARK 500 4 GLN A 20 47.16 -89.83
REMARK 500 4 PRO A 24 26.07 -76.14
REMARK 500 4 PHE A 64 -42.06 -139.31
REMARK 500 4 GLN A 83 -51.80 -127.91
REMARK 500 5 GLU A 5 156.67 71.17
REMARK 500 5 GLN A 20 40.28 -80.01
REMARK 500 5 GLN A 63 -51.82 -135.60
REMARK 500 6 ARG A 23 88.80 -153.55
REMARK 500 6 THR A 106 -152.77 -127.42
REMARK 500 7 SER A 26 -168.72 -124.37
REMARK 500 7 SER A 80 -80.85 -95.56
REMARK 500 7 THR A 116 -64.07 -95.07
REMARK 500 8 ASP A 107 -53.01 -144.57
REMARK 500 9 GLN A 20 29.96 -74.05
REMARK 500 9 PRO A 24 34.26 -92.03
REMARK 500 10 GLU A 54 -75.41 -89.24
REMARK 500 10 GLN A 63 -47.32 -133.50
REMARK 500 10 SER A 80 -169.62 -169.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 11588 RELATED DB: BMRB
REMARK 900 RELATED ID: 2RUQ RELATED DB: PDB
DBREF 2RUR A 5 117 UNP Q13526 PIN1_HUMAN 51 163
SEQADV 2RUR GLY A 1 UNP Q13526 EXPRESSION TAG
SEQADV 2RUR SER A 2 UNP Q13526 EXPRESSION TAG
SEQADV 2RUR HIS A 3 UNP Q13526 EXPRESSION TAG
SEQADV 2RUR MET A 4 UNP Q13526 EXPRESSION TAG
SEQADV 2RUR SER A 67 UNP Q13526 CYS 113 ENGINEERED MUTATION
SEQRES 1 A 117 GLY SER HIS MET GLU PRO ALA ARG VAL ARG CYS SER HIS
SEQRES 2 A 117 LEU LEU VAL LYS HIS SER GLN SER ARG ARG PRO SER SER
SEQRES 3 A 117 TRP ARG GLN GLU LYS ILE THR ARG THR LYS GLU GLU ALA
SEQRES 4 A 117 LEU GLU LEU ILE ASN GLY TYR ILE GLN LYS ILE LYS SER
SEQRES 5 A 117 GLY GLU GLU ASP PHE GLU SER LEU ALA SER GLN PHE SER
SEQRES 6 A 117 ASP SER SER SER ALA LYS ALA ARG GLY ASP LEU GLY ALA
SEQRES 7 A 117 PHE SER ARG GLY GLN MET GLN LYS PRO PHE GLU ASP ALA
SEQRES 8 A 117 SER PHE ALA LEU ARG THR GLY GLU MET SER GLY PRO VAL
SEQRES 9 A 117 PHE THR ASP SER GLY ILE HIS ILE ILE LEU ARG THR GLU
HELIX 1 1 THR A 35 GLY A 53 1 19
HELIX 2 2 ASP A 56 PHE A 64 1 9
HELIX 3 3 SER A 67 ARG A 73 5 7
HELIX 4 4 GLN A 85 LEU A 95 1 11
SHEET 1 A 4 ASP A 75 PHE A 79 0
SHEET 2 A 4 VAL A 9 VAL A 16 -1 N VAL A 9 O PHE A 79
SHEET 3 A 4 ILE A 110 GLU A 117 -1 O LEU A 114 N SER A 12
SHEET 4 A 4 GLU A 99 MET A 100 -1 N GLU A 99 O ARG A 115
SHEET 1 B 4 ASP A 75 PHE A 79 0
SHEET 2 B 4 VAL A 9 VAL A 16 -1 N VAL A 9 O PHE A 79
SHEET 3 B 4 ILE A 110 GLU A 117 -1 O LEU A 114 N SER A 12
SHEET 4 B 4 VAL A 104 PHE A 105 -1 N VAL A 104 O HIS A 111
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
(ATOM LINES ARE NOT SHOWN.)
END