HEADER ISOMERASE 02-APR-00 1EQ3
TITLE NMR STRUCTURE OF HUMAN PARVULIN HPAR14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS/TRANS ISOMERASE (PPIASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PPIASE DOMAIN (RESIDUES 36-131);
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 ORGAN: LUNG;
SOURCE 6 CELL: ENDOTHELIAL CELLS;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PQE70;
SOURCE 11 OTHER_DETAILS: HOMO SAPIENS
KEYWDS PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, PARVULIN, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR E.SEKERINA,U.J.RAHFELD,J.MULLER,G.FISCHER,P.BAYER
REVDAT 4 16-FEB-22 1EQ3 1 REMARK
REVDAT 3 24-FEB-09 1EQ3 1 VERSN
REVDAT 2 01-APR-03 1EQ3 1 JRNL
REVDAT 1 04-APR-01 1EQ3 0
JRNL AUTH E.SEKERINA,J.U.RAHFELD,J.MULLER,J.FANGHANEL,C.RASCHER,
JRNL AUTH 2 G.FISCHER,P.BAYER
JRNL TITL NMR SOLUTION STRUCTURE OF HPAR14 REVEALS SIMILARITY TO THE
JRNL TITL 2 PEPTIDYL PROLYL CIS/TRANS ISOMERASE DOMAIN OF THE MITOTIC
JRNL TITL 3 REGULATOR HPIN1 BUT INDICATES A DIFFERENT FUNCTIONALITY OF
JRNL TITL 4 THE PROTEIN.
JRNL REF J.MOL.BIOL. V. 301 1003 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10966801
JRNL DOI 10.1006/JMBI.2000.4013
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.UCHIDA,F.FUJIMORI,T.TRADLER,G.FISCHER,J.U.RAHFELD
REMARK 1 TITL IDENTIFICATION AND CHARACTERIZATION OF A 14KDA HUMAN PROTEIN
REMARK 1 TITL 2 AS A NOVEL PARVULIN-LIKE PEPTIDYL-PROLYL CIS/TRANS ISOMERASE
REMARK 1 REF FEBS LETT. V. 446 278 1999
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(99)00239-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 98
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER; MSI (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CONSTRAINTS USED FOR CALCULATION: TOTAL
REMARK 3 NUMBER OF NOES = 1042, INTRA-RESIDUAL = 120, LONG-RANGE = 397,
REMARK 3 MEDIUM-RANGE = 167, SEQUENTIAL = 358; COUPLING CONSTANTS = 71,
REMARK 3 HYDROGEN BONDS = 38.
REMARK 4
REMARK 4 1EQ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010807.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PARVULIN; 10MM PHOSPHATE
REMARK 210 BUFFER;; 1MM PARVULIN U15N/13C;
REMARK 210 10MM PHOSPHATE BUFFER;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 2D_15N_HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5, NDEE, AURELIA 2.5,
REMARK 210 X-PLOR 98, INSIGHT II 98
REMARK 210 METHOD USED : REFINEMENT WAS DONE USING X
REMARK 210 -PLOR98 SIMULATED ANNEALING
REMARK 210 PROTOCOL.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 O ARG A 87 HE21 GLN A 95 1.56
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 LYS A 59 -92.63 39.46
REMARK 500 1 SER A 60 -158.03 -129.48
REMARK 500 1 ARG A 87 -62.58 -107.55
REMARK 500 1 VAL A 91 -88.32 -154.03
REMARK 500 1 VAL A 110 -77.24 -133.28
REMARK 500 1 PRO A 115 -179.44 -69.38
REMARK 500 2 GLU A 46 -157.95 -55.23
REMARK 500 2 LYS A 59 -133.62 52.20
REMARK 500 2 LYS A 75 -35.62 -38.32
REMARK 500 2 GLN A 78 -77.78 62.61
REMARK 500 2 THR A 86 -92.99 -72.14
REMARK 500 2 MET A 90 -86.39 -141.65
REMARK 500 2 ASP A 107 -86.94 -144.23
REMARK 500 2 THR A 112 95.36 -48.87
REMARK 500 2 ARG A 130 -85.55 -132.41
REMARK 500 3 LYS A 59 161.09 -42.55
REMARK 500 3 ASP A 74 72.10 -102.07
REMARK 500 3 GLN A 78 99.94 33.92
REMARK 500 3 VAL A 91 -91.25 34.51
REMARK 500 3 LEU A 101 65.77 -106.03
REMARK 500 3 THR A 112 90.77 -58.26
REMARK 500 3 PHE A 120 43.26 -88.60
REMARK 500 4 ARG A 77 -18.39 81.14
REMARK 500 4 GLN A 78 177.33 70.38
REMARK 500 4 MET A 90 -83.04 -130.16
REMARK 500 4 ASP A 107 -62.93 -103.90
REMARK 500 4 VAL A 110 -99.63 -106.87
REMARK 500 4 ARG A 130 -35.69 -132.77
REMARK 500 5 LYS A 59 -134.42 23.41
REMARK 500 5 VAL A 67 -71.71 -62.74
REMARK 500 5 SER A 89 -62.16 -120.96
REMARK 500 5 MET A 90 -86.51 -137.44
REMARK 500 5 VAL A 103 90.98 -68.78
REMARK 500 5 ASP A 107 -46.85 -140.30
REMARK 500 5 VAL A 110 -74.73 -121.33
REMARK 500 5 THR A 112 -104.16 -62.15
REMARK 500 6 GLU A 46 -171.64 -64.76
REMARK 500 6 LYS A 59 -138.75 44.57
REMARK 500 6 ASP A 74 59.21 -104.43
REMARK 500 6 GLN A 78 -72.63 -143.45
REMARK 500 6 SER A 89 -32.09 -141.80
REMARK 500 6 MET A 90 -145.11 -104.33
REMARK 500 6 VAL A 110 -85.31 -144.86
REMARK 500 7 LYS A 59 -159.62 39.17
REMARK 500 7 ARG A 87 46.11 -98.96
REMARK 500 7 MET A 90 -166.15 -100.93
REMARK 500 7 ASP A 107 -59.09 -137.84
REMARK 500 7 THR A 112 97.38 -50.43
REMARK 500 8 LYS A 59 -99.06 45.83
REMARK 500 8 GLN A 78 105.46 -169.52
REMARK 500
REMARK 500 THIS ENTRY HAS 164 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 41 0.30 SIDE CHAIN
REMARK 500 1 ARG A 63 0.29 SIDE CHAIN
REMARK 500 1 ARG A 77 0.21 SIDE CHAIN
REMARK 500 1 ARG A 87 0.22 SIDE CHAIN
REMARK 500 1 ARG A 130 0.32 SIDE CHAIN
REMARK 500 2 ARG A 41 0.24 SIDE CHAIN
REMARK 500 2 ARG A 63 0.31 SIDE CHAIN
REMARK 500 2 ARG A 77 0.19 SIDE CHAIN
REMARK 500 2 ARG A 87 0.31 SIDE CHAIN
REMARK 500 3 ARG A 41 0.08 SIDE CHAIN
REMARK 500 3 ARG A 63 0.27 SIDE CHAIN
REMARK 500 3 ARG A 77 0.19 SIDE CHAIN
REMARK 500 3 ARG A 87 0.14 SIDE CHAIN
REMARK 500 3 ARG A 130 0.24 SIDE CHAIN
REMARK 500 4 ARG A 41 0.17 SIDE CHAIN
REMARK 500 4 ARG A 63 0.25 SIDE CHAIN
REMARK 500 4 ARG A 77 0.28 SIDE CHAIN
REMARK 500 4 ARG A 130 0.17 SIDE CHAIN
REMARK 500 5 ARG A 41 0.28 SIDE CHAIN
REMARK 500 5 ARG A 63 0.30 SIDE CHAIN
REMARK 500 5 ARG A 77 0.30 SIDE CHAIN
REMARK 500 5 ARG A 87 0.20 SIDE CHAIN
REMARK 500 5 ARG A 130 0.20 SIDE CHAIN
REMARK 500 6 ARG A 41 0.27 SIDE CHAIN
REMARK 500 6 ARG A 63 0.32 SIDE CHAIN
REMARK 500 6 ARG A 77 0.32 SIDE CHAIN
REMARK 500 6 ARG A 87 0.19 SIDE CHAIN
REMARK 500 6 ARG A 130 0.11 SIDE CHAIN
REMARK 500 7 ARG A 41 0.20 SIDE CHAIN
REMARK 500 7 ARG A 63 0.11 SIDE CHAIN
REMARK 500 7 ARG A 77 0.22 SIDE CHAIN
REMARK 500 7 ARG A 87 0.12 SIDE CHAIN
REMARK 500 7 ARG A 130 0.23 SIDE CHAIN
REMARK 500 8 ARG A 41 0.20 SIDE CHAIN
REMARK 500 8 ARG A 63 0.17 SIDE CHAIN
REMARK 500 8 ARG A 77 0.30 SIDE CHAIN
REMARK 500 8 ARG A 87 0.25 SIDE CHAIN
REMARK 500 8 ARG A 130 0.28 SIDE CHAIN
REMARK 500 9 ARG A 41 0.21 SIDE CHAIN
REMARK 500 9 ARG A 63 0.28 SIDE CHAIN
REMARK 500 9 ARG A 77 0.31 SIDE CHAIN
REMARK 500 9 ARG A 87 0.26 SIDE CHAIN
REMARK 500 9 ARG A 130 0.16 SIDE CHAIN
REMARK 500 10 ARG A 41 0.14 SIDE CHAIN
REMARK 500 10 ARG A 63 0.10 SIDE CHAIN
REMARK 500 10 ARG A 77 0.13 SIDE CHAIN
REMARK 500 10 ARG A 87 0.27 SIDE CHAIN
REMARK 500 10 ARG A 130 0.30 SIDE CHAIN
REMARK 500 11 ARG A 41 0.30 SIDE CHAIN
REMARK 500 11 ARG A 63 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 115 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PIN RELATED DB: PDB
REMARK 900 1PIN IS A STRUCTURAL RELATED HUMAN PARVULIN
DBREF 1EQ3 A 36 131 UNP Q9Y237 PIN4_HUMAN 36 131
SEQRES 1 A 96 ASN ALA VAL LYS VAL ARG HIS ILE LEU CYS GLU LYS HIS
SEQRES 2 A 96 GLY LYS ILE MET GLU ALA MET GLU LYS LEU LYS SER GLY
SEQRES 3 A 96 MET ARG PHE ASN GLU VAL ALA ALA GLN TYR SER GLU ASP
SEQRES 4 A 96 LYS ALA ARG GLN GLY GLY ASP LEU GLY TRP MET THR ARG
SEQRES 5 A 96 GLY SER MET VAL GLY PRO PHE GLN GLU ALA ALA PHE ALA
SEQRES 6 A 96 LEU PRO VAL SER GLY MET ASP LYS PRO VAL PHE THR ASP
SEQRES 7 A 96 PRO PRO VAL LYS THR LYS PHE GLY TYR HIS ILE ILE MET
SEQRES 8 A 96 VAL GLU GLY ARG LYS
HELIX 1 1 LYS A 50 LYS A 59 1 10
HELIX 2 2 ARG A 63 SER A 72 1 10
HELIX 3 3 GLY A 92 LEU A 101 1 10
SHEET 1 A 4 ASP A 81 MET A 85 0
SHEET 2 A 4 VAL A 38 CYS A 45 -1 O VAL A 38 N MET A 85
SHEET 3 A 4 GLY A 121 GLY A 129 -1 O TYR A 122 N CYS A 45
SHEET 4 A 4 VAL A 116 THR A 118 -1 O VAL A 116 N HIS A 123
CISPEP 1 ASP A 113 PRO A 114 1 -0.15
CISPEP 2 ASP A 113 PRO A 114 2 0.30
CISPEP 3 ASP A 113 PRO A 114 3 0.09
CISPEP 4 ASP A 113 PRO A 114 4 -0.42
CISPEP 5 ASP A 113 PRO A 114 5 1.31
CISPEP 6 ASP A 113 PRO A 114 6 -0.21
CISPEP 7 ASP A 113 PRO A 114 7 1.25
CISPEP 8 ASP A 113 PRO A 114 8 0.12
CISPEP 9 ASP A 113 PRO A 114 9 2.07
CISPEP 10 ASP A 113 PRO A 114 10 -0.45
CISPEP 11 ASP A 113 PRO A 114 11 0.63
CISPEP 12 ASP A 113 PRO A 114 12 0.69
CISPEP 13 ASP A 113 PRO A 114 13 -0.09
CISPEP 14 ASP A 113 PRO A 114 14 0.86
CISPEP 15 ASP A 113 PRO A 114 15 0.54
CISPEP 16 ASP A 113 PRO A 114 16 0.40
CISPEP 17 ASP A 113 PRO A 114 17 1.82
CISPEP 18 ASP A 113 PRO A 114 18 0.44
CISPEP 19 ASP A 113 PRO A 114 19 -0.04
CISPEP 20 ASP A 113 PRO A 114 20 0.13
CISPEP 21 ASP A 113 PRO A 114 21 0.28
CISPEP 22 ASP A 113 PRO A 114 22 -0.51
CISPEP 23 ASP A 113 PRO A 114 23 -0.34
CISPEP 24 ASP A 113 PRO A 114 24 -0.29
CISPEP 25 ASP A 113 PRO A 114 25 1.53
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
