Header list of 1fjd.pdb file
Complete list - v 3 2 Bytes
HEADER ISOMERASE 08-AUG-00 1FJD
TITLE HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL PROLYL CIS/TRANS ISOMERASE (PPIASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 28-131;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS PARVULIN, PEPTIDYL PROLYL CIS/TRANS ISOMERASE, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR T.TERADA,M.SHIROUZU,Y.FUKUMORI,F.FUJIMORI,Y.ITO,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 T.UCHIDA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 03-NOV-21 1FJD 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1FJD 1 VERSN
REVDAT 1 08-AUG-01 1FJD 0
JRNL AUTH T.TERADA,M.SHIROUZU,Y.FUKUMORI,F.FUJIMORI,Y.ITO,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA,T.UCHIDA
JRNL TITL SOLUTION STRUCTURE OF THE HUMAN PARVULIN-LIKE PEPTIDYL
JRNL TITL 2 PROLYL CIS/TRANS ISOMERASE, HPAR14.
JRNL REF J.MOL.BIOL. V. 305 917 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11162102
JRNL DOI 10.1006/JMBI.2000.4293
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AZARA 2.0, X-PLOR 3.1
REMARK 3 AUTHORS : BOUCHER, W. (AZARA), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FLOATING CHIRALITY METHOD WAS USED TO
REMARK 3 DETERMINE THE STRUCTURE OF PROCHIRAL METHYLENES AND METHYLS.
REMARK 4
REMARK 4 1FJD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011637.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM HPAR14 U-15N,13C; 20MM
REMARK 210 SODIUM PHOSPHATE BUFFER; 100MM
REMARK 210 NACL; 5MM DTT; 90% H2O, 10% D2O;
REMARK 210 2MM HPAR14 U-15N; 20MM SODIUM
REMARK 210 PHOSPHATE BUFFER; 100MM NACL;
REMARK 210 5MM DTT; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING METHOD
REMARK 210 STARTING WITH AN EXTENDED STRAND
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 : 20
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D TRIPLE
REMARK 210 RESONANCE TECHNIQUES.
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 GLN A 70 H GLU A 73 1.39
REMARK 500 O MET A 52 H GLU A 56 1.49
REMARK 500 O CYS A 45 HD1 HIS A 48 1.54
REMARK 500 O LYS A 50 H ALA A 54 1.55
REMARK 500 O CYS A 45 H HIS A 48 1.56
REMARK 500 O ILE A 43 H ILE A 124 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 PRO A 31 90.37 -61.73
REMARK 500 1 HIS A 48 16.02 56.66
REMARK 500 1 MET A 62 -141.58 -82.42
REMARK 500 1 ALA A 69 -72.76 -64.18
REMARK 500 1 GLU A 73 42.71 29.42
REMARK 500 1 ASP A 74 -138.84 179.53
REMARK 500 1 LYS A 75 -90.99 -57.09
REMARK 500 1 ALA A 76 152.55 167.64
REMARK 500 1 ARG A 77 -65.76 -94.04
REMARK 500 1 GLN A 78 -89.87 -60.18
REMARK 500 1 ASP A 81 94.94 -41.22
REMARK 500 1 LEU A 82 -76.27 -40.40
REMARK 500 1 MET A 90 -66.66 -107.35
REMARK 500 1 VAL A 91 -89.86 174.43
REMARK 500 1 ALA A 97 -81.19 -86.18
REMARK 500 1 ALA A 98 -71.57 -39.97
REMARK 500 1 VAL A 103 159.87 -41.39
REMARK 500 1 SER A 104 -143.48 -179.45
REMARK 500 1 MET A 106 -169.27 65.86
REMARK 500 1 LYS A 108 52.21 -141.53
REMARK 500 1 PRO A 109 -151.64 -65.96
REMARK 500 1 VAL A 110 -160.62 -78.90
REMARK 500 1 THR A 112 -161.74 -62.02
REMARK 500 1 PRO A 115 77.01 -67.23
REMARK 500 1 THR A 118 -44.77 -159.84
REMARK 500 1 LYS A 119 27.68 -175.34
REMARK 500 1 PHE A 120 25.14 -170.09
REMARK 500 2 PRO A 31 96.42 -61.56
REMARK 500 2 LYS A 32 78.21 -150.85
REMARK 500 2 HIS A 48 15.63 56.97
REMARK 500 2 LYS A 59 -76.85 -73.67
REMARK 500 2 MET A 62 -147.07 -86.30
REMARK 500 2 ASP A 74 15.49 58.20
REMARK 500 2 ALA A 76 148.48 68.14
REMARK 500 2 ARG A 77 -61.45 -100.67
REMARK 500 2 ASP A 81 94.95 -38.35
REMARK 500 2 ARG A 87 89.76 -63.86
REMARK 500 2 MET A 90 -140.29 -67.05
REMARK 500 2 VAL A 91 -153.00 -124.61
REMARK 500 2 GLU A 96 -75.42 -41.73
REMARK 500 2 ALA A 98 -77.67 -95.83
REMARK 500 2 PRO A 102 178.64 -59.16
REMARK 500 2 SER A 104 -34.58 168.31
REMARK 500 2 MET A 106 31.88 80.10
REMARK 500 2 ASP A 107 78.38 35.79
REMARK 500 2 LYS A 108 -52.77 175.05
REMARK 500 2 PRO A 109 -73.99 -69.91
REMARK 500 2 VAL A 110 179.96 -47.88
REMARK 500 2 THR A 112 -169.96 -52.16
REMARK 500 2 PRO A 115 75.90 -65.82
REMARK 500
REMARK 500 THIS ENTRY HAS 513 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 0.10 SIDE CHAIN
REMARK 500 1 ARG A 63 0.29 SIDE CHAIN
REMARK 500 1 ARG A 77 0.20 SIDE CHAIN
REMARK 500 1 ARG A 87 0.12 SIDE CHAIN
REMARK 500 1 ARG A 130 0.18 SIDE CHAIN
REMARK 500 2 ARG A 41 0.16 SIDE CHAIN
REMARK 500 2 ARG A 63 0.21 SIDE CHAIN
REMARK 500 2 ARG A 77 0.12 SIDE CHAIN
REMARK 500 2 ARG A 87 0.26 SIDE CHAIN
REMARK 500 2 ARG A 130 0.28 SIDE CHAIN
REMARK 500 3 ARG A 41 0.26 SIDE CHAIN
REMARK 500 3 ARG A 63 0.22 SIDE CHAIN
REMARK 500 3 ARG A 77 0.18 SIDE CHAIN
REMARK 500 3 ARG A 87 0.22 SIDE CHAIN
REMARK 500 3 ARG A 130 0.29 SIDE CHAIN
REMARK 500 4 ARG A 41 0.29 SIDE CHAIN
REMARK 500 4 ARG A 63 0.09 SIDE CHAIN
REMARK 500 4 ARG A 77 0.21 SIDE CHAIN
REMARK 500 4 ARG A 87 0.24 SIDE CHAIN
REMARK 500 4 ARG A 130 0.30 SIDE CHAIN
REMARK 500 5 ARG A 41 0.32 SIDE CHAIN
REMARK 500 5 ARG A 63 0.32 SIDE CHAIN
REMARK 500 5 ARG A 77 0.12 SIDE CHAIN
REMARK 500 5 ARG A 87 0.32 SIDE CHAIN
REMARK 500 5 ARG A 130 0.31 SIDE CHAIN
REMARK 500 6 ARG A 41 0.15 SIDE CHAIN
REMARK 500 6 ARG A 63 0.20 SIDE CHAIN
REMARK 500 6 ARG A 77 0.24 SIDE CHAIN
REMARK 500 6 ARG A 87 0.32 SIDE CHAIN
REMARK 500 6 ARG A 130 0.28 SIDE CHAIN
REMARK 500 7 ARG A 41 0.29 SIDE CHAIN
REMARK 500 7 ARG A 63 0.21 SIDE CHAIN
REMARK 500 7 ARG A 77 0.32 SIDE CHAIN
REMARK 500 7 ARG A 87 0.30 SIDE CHAIN
REMARK 500 7 ARG A 130 0.29 SIDE CHAIN
REMARK 500 8 ARG A 41 0.22 SIDE CHAIN
REMARK 500 8 ARG A 63 0.31 SIDE CHAIN
REMARK 500 8 ARG A 77 0.20 SIDE CHAIN
REMARK 500 8 ARG A 87 0.21 SIDE CHAIN
REMARK 500 8 ARG A 130 0.26 SIDE CHAIN
REMARK 500 9 ARG A 41 0.27 SIDE CHAIN
REMARK 500 9 ARG A 63 0.18 SIDE CHAIN
REMARK 500 9 ARG A 77 0.32 SIDE CHAIN
REMARK 500 9 ARG A 87 0.27 SIDE CHAIN
REMARK 500 9 ARG A 130 0.32 SIDE CHAIN
REMARK 500 10 ARG A 41 0.18 SIDE CHAIN
REMARK 500 10 ARG A 63 0.30 SIDE CHAIN
REMARK 500 10 ARG A 77 0.13 SIDE CHAIN
REMARK 500 10 ARG A 87 0.32 SIDE CHAIN
REMARK 500 10 ARG A 130 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 97 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NHS001015441.1 RELATED DB: TARGETDB
DBREF 1FJD A 28 131 UNP Q9Y237 PIN4_HUMAN 28 131
SEQADV 1FJD GLY A 28 UNP Q9Y237 ALA 28 ENGINEERED MUTATION
SEQADV 1FJD SER A 29 UNP Q9Y237 GLN 29 ENGINEERED MUTATION
SEQRES 1 A 104 GLY SER GLY PRO LYS GLY GLY GLY ASN ALA VAL LYS VAL
SEQRES 2 A 104 ARG HIS ILE LEU CYS GLU LYS HIS GLY LYS ILE MET GLU
SEQRES 3 A 104 ALA MET GLU LYS LEU LYS SER GLY MET ARG PHE ASN GLU
SEQRES 4 A 104 VAL ALA ALA GLN TYR SER GLU ASP LYS ALA ARG GLN GLY
SEQRES 5 A 104 GLY ASP LEU GLY TRP MET THR ARG GLY SER MET VAL GLY
SEQRES 6 A 104 PRO PHE GLN GLU ALA ALA PHE ALA LEU PRO VAL SER GLY
SEQRES 7 A 104 MET ASP LYS PRO VAL PHE THR ASP PRO PRO VAL LYS THR
SEQRES 8 A 104 LYS PHE GLY TYR HIS ILE ILE MET VAL GLU GLY ARG LYS
HELIX 1 A1 MET A 52 LYS A 59 1 8
HELIX 2 A2 PHE A 64 TYR A 71 1 8
HELIX 3 A3 PRO A 93 ALA A 97 1 5
SHEET 1 SH1 4 MET A 85 THR A 86 0
SHEET 2 SH1 4 ALA A 37 LEU A 44 -1 N VAL A 38 O MET A 85
SHEET 3 SH1 4 TYR A 122 GLU A 128 -1 N ILE A 124 O ILE A 43
SHEET 4 SH1 4 VAL A 116 LYS A 117 -1 N VAL A 116 O HIS A 123
CRYST1 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 - v 3 2 Bytes